WO2023021331A1

WO2023021331A1 - Jack fruit protein concentrates

Info

Publication number: WO2023021331A1
Application number: PCT/IB2022/000465
Authority: WO
Inventors: Bryony TINN-DISBURY; Jennifer PARDOE
Original assignee: Willaroos Ltd (Trading As Jack & Bry)
Priority date: 2021-08-18
Filing date: 2022-08-17
Publication date: 2023-02-23

Abstract

The present invention provides methods for making protein concentrates from jackfruit seeds, jackfruit seed protein compositions, and food products containing jackfruit seed proteins.

Description

JACK FRUIT PROTEIN CONCENTRATES CROSS-REFERENCE TO RELATED APPLICATION The present application claims priority to U.S. Provisional Patent Application No. 63/234,313, filed August 18, 2021, which is hereby incorporated by reference in its entirety. FIELD OF THE INVENTION The present invention provides methods for making protein concentrates from jackfruit seeds, jackfruit seed protein compositions, and food products containing jackfruit seed proteins. BACKGROUND OF THE INVENTION Jackfruit (Artocarpus heterophyllus L.) is a tree belonging to the family Moraceae and is widely distributed in tropical countries such as Brazil, Bangladesh, Indonesia, the Philippines and Malaysia (Ulloa et al., 201; Madruga et al., 2014). Once it easily proliferates in warmer regions, jackfruit can also be cultivated throughout the tropical coast of Mexico (Ulloa et al., 2017). Ripe jackfruits are large sized fruits measuring between 22–90 cm in length and 13–50 cm in diameter with weight ranging from 2–36 kg (Mahanta and Kalita, 2015). The fruit may contain between 100 and 500 seeds which represents 18–25% (in dry basis) of the fruit weight while the pulp represents 30% of the fruit weight (Madrigal-Aldrina et al., 2011). The raw fruit is eaten as a vegetable. Ripened jackfruit pulp is eaten both in raw and processed forms like canned juice (Seow and Sanmugam, 1992), and fruit leather. The pulp is cream in color due to the presence of carotenoids. The residues after processing of jackfruit can constitute up to 70% of the total weight of the fruit (Ulloa et al., 2017). The shape of the seeds of the ripe fruit varies from oval to oblong ellipsoidal to round. The seeds are light brown in colour and are generally 2–3 cm in length and 1–1.5 cm in diameter. Seeds of the ripe fruit have around 55% moisture and therefore do not keep well for long. Traditionally, the majority of the seeds are discarded in the environment, although a little portion is consumed after minimal processing like roasting and boiling (Haque et al., 2020). Jackfruit seeds (JFS) are a good source of starch (22%) and dietary fiber (3.19%) Additionally, JFS contains lignans, isoflavones and saponins, which are all phytonutrients that have health benefits that are wide-ranging from anticancer to antihypertensive antiaging antioxidant and antiulcer (Omale & Friday, 2010). In recent years there has been a growing search for alternative sources of protein and starch to meet industry demands, because of which JFS is gaining the attention of researchers (Mahanta and Kalita, 2015). The average chemical composition of JFSs was shown in Table 1. The reported values for the constituents in JFS seem to vary mainly due to variations related with differences in source, variety, environment, and ripeness of the fruit (Mahanta and Kalita, 2015). Nonetheless, the seed is a fairly good source of starch and protein. Table 1. Chemical composition of JFS.

Proteins are present in jackfruit seeds with a composition that ranges between 17.8 and 37% depending on the variety of jackfruit (Swami et al., 2012). A study performed by Kumar et al. (1982) on JFSs found that it contained lectin, a class of glycoproteins which has been reported to possess antibacterial, antifungal and anticarcinogenic properties. Lectins are considered to be antinutritional as they bind with carbohydrates and escape digestion (Mahanta and Kalita, 2015). However, thermal treatment prior to consumption reduces/destroys the antinutritional factors in the seed by protein denaturation. More than 50% of the protein in JFS is comprised of jacalin, a lectin having molecular weight of 65 kDa. Jacalin is a tetramer with two chains, the α-chain with 133 amino acids and the β-chain with 20–21 amino acids (Kabir, 1998). It has been studied for capturing O- glycoproteins such as mucins and IgA1, for potential applications in human immunology. Jacalin is preferably used in applications to isolate IgA from human serum, isolating human plasma glycoproteins and for applications in histochemistry. In a study on Jacalin protein isolation, Kabir (1995) employed a phosphate-buffered saline (PBS, 0.01 M, pH = 7.4) to extract the proteins from JFSs. They mixed the PBS solution with ground JFS and kept constant stirring at 4 °C for 24 h. After centrifugation and filtration, the protein extract was purified by ion-exchange chromatography. The extracted protein had its structure preserved and still presented biological activity as it agglutinated erythrocytes. The extraction yield of the protein, however, was not reported. Alkaline extraction followed by acid precipitation is the traditional way of extracting vegetable protein and high yield and purity proteins can be obtained by using this method (Hou et al., 2017; Jangchud and Chinnan, 1999). Additionally, this method is simple and suitable for low- cost mass production making it one of the main industrial protein producing techniques. JFS alkaline extraction with NaOH has been widely reported in the literature (Ulloa et al., 2017; Zhang et al.2019; Akter et al., 2020; Haque et al., 2020). However, there is an overall lack of extraction yields being reported. Additionally, there are some discrepancies in the literature related with the protein solubility in alkaline medium. In a study of JFS flour protein extraction, Ulloa et al., (2017) found the optimal pH of extraction to be close to 12, in which the protein solubility reached up to 80 wt%. Whereas Zhang et al. (2019), by studying JFS protein isolates, found lower solubility values for the alkaline range (7-9). Such differences may arise due to differences in the feedstock composition and in the protein constitution. The majority of works (Ulloa et al., 2017; Zhang et al.2019; Akter et al., 2020; Haque et al., 2020) employed mild alkaline conditions, i.e., low alkali concentration (0.1 to 1 M NaOH), low temperatures (room temperature) and short extraction times (from 30 to 60 min). Reverse micelles are a recently new alternative to protein liquid–liquid extraction methods from JFS. They are nanometric size molecular aggregates of surfactants, with their polar head groups concentrated in the interior, while their hydrophobic tale extends into and are surrounded by the organic solvent (Reis et al., 2016). They can constitute thermodynamically stable and optically transparent systems (Reis et al., 2016; Silber, Biasutti, Abuin, & Lissi, 1999; Nandini & Rastogi, 2009). This method presents several advantages such as low interfacial tension, ease of scale-up and continuous mode of operation. The biotechnological importance of reverse micelles is owed to their capacity of increasing the solubility of hydrophilic molecules, such as proteins, by interacting with their polar sites (Sun, Zhu, & Zhou, 2008). Reis et al. (2016) developed this alternative method for protein extraction from jackfruit seed flour using reverse micelles, with sodium dodecyl sulphate (SDS) as surfactant and butanol as organic solvent. SDS is an anionic surfactant and an FDA-approved food additive (FDA 21 CFR 172.822) (Predmore & Li, 2011). Based on the analysis of surface response methodology the best extraction yield was obtained at 25°C stirring time of 120 min, mass of flour of 100 mg, and a ratio H2O:SDS-1 of 50. Experimental results showed that a 79.00% extraction yield could be obtained. What is needed in the art are more selective processes for extracting high-quality jackfruit seed protein. SUMMARY OF THE INVENTION The present invention provides methods for making protein concentrates from jackfruit seeds, jackfruit seed protein compositions, and food products containing jackfruit seed proteins. For example, in some embodiments, provided herein is a process for extracting a protein concentrate from jackfruit seed comprising: processing jackfruit seed to provide a jackfruit seed composition with reduced particle size; treating the jackfruit seed composition with reduced particle size with a solution comprising an amine (e.g., monoethanolamine or choline hydroxide) to provide a mixture with a solid phase and a liquid phase comprising jackfruit seed protein; and recovering a jackfruit seed protein concentrate from the liquid phase. In some preferred embodiments, the step of treating the jackfruit seed composition with reduced particle size with a solution comprising an amine to provide a mixture with a solid phase and a liquid phase comprising jackfruit seed protein comprises adding the amine to a concentration of from 0.02 to 0.06 mol/L in the liquid phase. In some preferred embodiments, the process provides a protein yield of from 45% to 55%. Certain aspects of the process include additional steps, for example, defatting the jackfruit seed composition with reduced particle size prior to treating the jackfruit seed composition with reduced particle size with a solution comprising an amine, recovering the jackfruit seed protein concentrate from the liquid phase comprises isoelectric precipitation, and/or drying the recovered jackfruit seed protein concentrate. In some preferred embodiments, the present invention provides processes for extracting a protein concentrate from jackfruit seed comprising: processing jackfruit seed to provide a jackfruit seed composition with reduced particle size; treating the jackfruit seed composition with reduced particle size with a solution comprising an alkali to provide a mixture with a solid phase and a liquid phase comprising jackfruit seed protein, wherein the alkali is added to a concentration of from 0.02 to 0.06 mol/L; and recovering the jackfruit seed protein concentrate from the liquid phase In some preferred embodiments, the alkali is added to a concentration of from 0.03 to 0.05 mol/L. In some preferred embodiments, the alkali is added to a concentration of from 0.035 to 0.045 mol/L. In some preferred embodiments, the alkali is selected from the group consisting of sodium hydroxide, monoethanolamine, and choline hydroxide. In some preferred embodiments, the amine is choline hydroxide. In some preferred embodiments, the pH of the solution comprising an amine is from pH 7.0 to 12.0. In some preferred embodiments, the pH of the solution comprising an amine is from pH 8.0 to 10.0. In some preferred embodiments, the jackfruit seed protein concentrate produced by the process is characterized by having one or more of the following properties: a) a foaming capacity of from 50% to 80% at pH 7.0; b) a foaming stability of greater than 70% at pH 7.0; c) an emulsion activity of from 60% to 80% at pH 7.0; d) an emulsion stability of greater than 70% at pH 7.0; e) an oil holding capacity of from 1.8 to 2.5 gram oil/gram protein; f) an essential amino acid content of from 22 to 34%; g) a phenylalanine content of from 4.5% to 5.5%; and h) a methionine content of from 3.6% to 4.6%. In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having two or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having three or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having four or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having five or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having six or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having seven or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having all eight of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is further characterized as having a protein content of from 70% to 80% on a dry weight basis. In some embodiments, the recovered jackfruit seed protein concentrate is formulated with one or more additional proteins, lipids or carbohydrates (e.g., a separate preparation from jackfruit and/or from a source other than jackfruit). Also provide is a further step of producing a food product from the formulation (e.g., a meat substitute). Further embodiments provide a jackfruit seed protein concentrate or jackfruit seed protein concentrate formulation produced according to a process described herein. Additional embodiments provide a food product or multicomponent food composition produced according to a process described herein. In some embodiments, the composition is characterized in comprising from 0.1% to 50% (w/w), 0.1% to 20% (w/w), 0.1% to 10% (w/w), or 0.1% to 5% (w/w) of the jackfruit seed protein concentrate. In some embodiments, the multicomponent food composition comprises between 10-30% w/w protein, between 5- 80% w/w water, and between 5-70% fat. In some embodiments, the composition further comprises an additional plant protein (e.g., from a source other than jackfruit, e.g., proteins from grains, oil seeds, leafy greens, biomass crops, root vegetables, or legumes). Exemplary grains include but are not limited to corn, maize, rice, wheat, barley, rye, triticale or teff. Exemplary oil seeds include but are not limited to cottonseed, sunflower seed, safflower seed, or rapeseed. Exemplary leafy green include but are not limited to lettuce, spinach, kale, collard greens, turnip greens, chard, mustard greens, dandelion greens, broccoli, or cabbage. Exemplary biomass crops include but are not limited to switchgrass, miscanthus, sorghum, alfalfa, corn stover, green matter, sugar cane leaves or leaves of trees. Exemplary root crops include but are not limited to selected from the group consisting of cassava, sweet potato, potato, carrots, beets, and turnips. Exemplary legumes include but are not limited to selected from the group consisting of clover, cowpeas, English peas, yellow peas, green peas, soybeans, fava beans, lima beans, kidney beans, garbanzo beans, mung beans, pinto beans, lentils, lupins, mesquite, carob, soy, and peanuts, vetch (vicia), stylo (stylosanthes), arachis, indigofera, acacia, leucaena, cyamopsis, or sesbania. In some embodiments, the multicomponent food composition further comprises a fat (e.g., including but are not limited to corn oil, olive oil, soy oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flax seed oil, algal oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, an oil produced by bacteria, an oil produced by archaea, an oil produced by fungi, an oil produced by genetically engineered bacteria, an oil produced by genetically engineered algae, an oil produced by genetically engineered archaea, or an oil produced by genetically engineered fungi, and a mixture of two or more thereof. In still further preferred embodiments, the present invention provides a jackfruit seed protein concentrate characterized by having one or more of the following properties: a) a foaming capacity of from 50% to 80% at pH 7.0; b) a foaming stability of greater than 70% at pH 7.0; c) an emulsion activity of from 60% to 80% at pH 7.0; d) an emulsion stability of greater than 70% at pH 70; e) an oil holding capacity of from 18 to 25 gram oil/gram protein; f) an essential amino acid content of from 22 to 34%; g) a phenylalanine content of from 4.5% to 5.5%; and h) a methionine content of from 3.6% to 4.6%. In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having two or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having three or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having four or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having five or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having six or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having seven or more of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is characterized by having all eight of properties a) to h). In some preferred embodiments, the jackfruit seed protein concentrate is further characterized as having a protein content of from 70% to 80% on a dry weight basis. In some preferred embodiments, the present invention provides a multicomponent food composition comprising the jackfruit seed protein concentrate as described above. In some preferred embodiments, the composition is characterized in comprising from 0.1% to 50% (w/w), 0.1% to 20% (w/w), 0.1% to 10% (w/w), or 0.1% to 5% (w/w) of the jackfruit seed protein concentrate. In some preferred embodiments, the food composition further comprises an additional plant protein. In some preferred embodiments, additional plant protein is from a source other than jackfruit. In some preferred embodiments, the additional plant protein is selected from the group consisting of proteins from grains, oil seeds, leafy greens, biomass crops, root vegetables, and legumes. In some preferred embodiments, the grains are selected from the group consisting of corn, maize, rice, wheat, barley, rye, triticale and teff. In some preferred embodiments, the oilseeds are selected from the group consisting of cottonseed, sunflower seed, safflower seed, and rapeseed. In some preferred embodiments, the leafy greens are selected from the group consisting of lettuce, spinach, kale, collard greens, turnip greens, chard, mustard greens, dandelion greens, broccoli, and cabbage. In some preferred embodiments, the biomass crops are selected from the group consisting of switchgrass, miscanthus, sorghum, alfalfa, corn stover, green matter, sugar cane leaves and leaves of trees. In some preferred embodiments, the root crops are selected from the group consisting of cassava, sweet potato, potato, carrots, beets, and turnips. In some preferred embodiments the legumes are selected from the group consisting of clover cowpeas English peas, yellow peas, green peas, soybeans, fava beans, lima beans, kidney beans, garbanzo beans, mung beans, pinto beans, lentils, lupins, mesquite, carob, soy, and peanuts, vetch (vicia), stylo (stylosanthes), arachis, indigofera, acacia, leucaena, cyamopsis, and sesbania. In some preferred embodiments, the food composition further comprises a fat, preferably from a source other than jackfruit. In some preferred embodiments, the fat is selected from the group consisting of corn oil, olive oil, soy oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flax seed oil, algal oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, an oil produced by bacteria, an oil produced by archaea, an oil produced by fungi, an oil produced by genetically engineered bacteria, an oil produced by genetically engineered algae, an oil produced by genetically engineered archaea, and an oil produced by genetically engineered fungi, and a mixture of two or more thereof. In some preferred embodiments, the food compositions are further characterized in comprising between 10-30% w/w protein, between 5-80% w/w water, and between 5-70% fat. Additional embodiments are described herein. BRIEF DESCRIPTION OF THE DRAWINGS Fig.1. JFS chemical composition on a dry basis. Fig.2. Protein purity and yield as a function of extraction temperature, time and alkali concentration for (a) NaOH (b) ChOH. Fig.3. Protein yield and purity for the sequential washing experiments with dilute solutions of NaOH (a) and ChOH (b). An assay with the mixture of 0.25 mol/L ChOH and 0.25 mol/L MEA (depicted in purple) is also shown. Fig.4. Mass balance for the NaOH dilute extraction of JFS. Fig.5. Mass balance for the ChOH dilute extraction of JFS. Fig.6. Foaming capacity and stability for the JFSP concentrates extracted with ChOH, NaOH and for the commercial pea and soy protein isolates. Fig.7. Comparison between foaming capacity and stability values obtained in this study and Akter et al. (2020). Fig.8. Solubility of Pea PC, Soy PC, ChOH and NaOH JFSPC as a function of pH. Fig.9. Emulsion activity and stability for soy, pea, ChOH and NaOH protein concentrates. Fig.10. Mean (±SEM) phenylalanine (a) and methionine (b) contents (% of total protein) of various dietary protein sources and human skeletal muscle protein. White bars represent plant- based protein sources, grey bars represent animal-derived protein sources, and the black bar represents human muscle. The dashed line represents the amino acid requirements for adults (data from Gorissen et al. (2018) [46]). DEFINITIONS As used herein, term “foaming capacity” refers to the percentage calculated by dividing foam volume by initial sample volume where 0.5 g of JFSPC is diluted with 50 mL of a buffered solution at a defined pH (e.g., 4, 7 or 10), stirred and homogenized in a blender for 1.5 minutes, and measuring volume of foam in a measuring cylinder no later than 30 seconds after homogenization. As used herein, term “foaming stability” refers to the percentage calculated by dividing foam volume by initial sample volume where 0.5 g of JFSPC is diluted with 50 mL of a buffered solution at a defined pH (e.g., 4, 7 or 10), stirred and homogenized in a blender for 1.5 minutes, and measuring volume of foam in a measuring cylinder 30 minutes after homogenization As used herein, term “emulsion capacity” refers to the percentage calculated by dividing cream volume by initial sample volume, where 1 gram of protein isolate (e.g., JFSPC) is dissolved in 30 ml of phosphate-citrus buffer at a defined pH (e.g., 4, 7 or 10) to form a suspension, the suspension is mixed with 30 ml rapeseed oil, blended for 1.5 minutes and centrifuged at 1190 X G for 5 min. As used herein, term “emulsion stability” refers to the percentage calculated by dividing crema volume after 3 hours by initial cream volume, where the emulsions are prepared by dissolving 1 g of protein isolate in 30 ml of phosphate-citrate buffer at a specified pH (i.e., pH 4, 7 or 10), adding 30 ml rapeseed oil, stirring in a blender for 1.5 minutes and centrifuging at 1190 X g for 5 minutes. The cream value is determined initially and after 3 hours. DETAILED DESCRIPTION OF THE INVENTION The present invention provides methods for making protein concentrates from jackfruit seeds, jackfruit seed protein compositions, and food products containing jackfruit seed proteins. In some exemplary embodiments, protein concentrates are prepared using a method, comprising processing jackfruit seed to provide a jackfruit seed composition with reduced particle size; treating the jackfruit seed composition with reduced particle size with a solution comprising an amine (e.g., monoethanolamine or choline hydroxide) to provide a mixture with a solid phase and a liquid phase comprising jackfruit seed protein; and recovering a jackfruit seed protein concentrate from the liquid phase. Exemplary extraction protocols are described, for example, in Examples 1 and 2. The jackfruit seed protein concentrates (JFSPC) of the present invention may characterized by a number of properties. In some preferred embodiments, the JFSPC is characterized in: a) having a foaming capacity of from 50% to 80% at pH 7.0; b) having a foaming stability of greater than 70% at pH 7.0; c) having an emulsion activity of from 60% to 80% at pH 7.0; d) having an emulsion stability of greater than 70% at pH 7.0; e) having an oil holding capacity of from 1.8 to 2.5 gram oil/gram protein; f) having an essential amino acid content of from 22 to 34%; g) having a phenylalanine content of from 4.5% to 5.5%; h) having a methionine content of from 3.6% to 4.6%; and/or i) having a protein content of from 70% to 80% on a dry weight basis In some preferred embodiments, the JFSPC is characterized in any one of a) to i) above. In some preferred embodiments, the JFSPC is characterized in any two of a) to i) above. In some preferred embodiments, the JFSPC is characterized in any three of a) to i) above. In some preferred embodiments, the JFSPC is characterized in any four of a) to i) above. In some preferred embodiments, the JFSPC is characterized in any five of a) to i) above. In some preferred embodiments, the JFSPC is characterized in any six of a) to i) above. In some preferred embodiments, the JFSPC is characterized in any seven of a) to i) above. In some preferred embodiments, the JFSPC is characterized in any eight of a) to i) above. In some preferred embodiments, the JFSPC is characterized in all nine of a) to i) above. In some preferred embodiments, the JFSPC is characterized in a) and b) above. In some preferred embodiments, the JFSPC is characterized in a) and c) above. In some preferred embodiments the JFSPC is characterized in a) and d) above. In some preferred embodiments, the JFSPC is characterized in a) and e) above. In some preferred embodiments, the JFSPC is characterized in a) and f) above. In some preferred embodiments, the JFSPC is characterized in a) and g) above. In some preferred embodiments, the JFSPC is characterized in a) and h) above. In some preferred embodiments, the JFSPC is characterized in a) and i) above. In some preferred embodiments, the JFSPC is characterized in b) and c) above. In some preferred embodiments, the JFSPC is characterized in b) and d) above. In some preferred embodiments, the JFSPC is characterized in b) and e) above. In some preferred embodiments, the JFSPC is characterized in b) and f) above. In some preferred embodiments, the JFSPC is characterized in b) and g) above. In some preferred embodiments, the JFSPC is characterized in b) and h) above. In some preferred embodiments, the JFSPC is characterized in b) and i) above. In some preferred embodiments, the JFSPC is characterized in c) and d) above. In some preferred embodiments, the JFSPC is characterized in c) and e) above. In some preferred embodiments, the JFSPC is characterized in c) and f) above. In some preferred embodiments, the JFSPC is characterized in c) and g) above. In some preferred embodiments, the JFSPC is characterized in c) and h) above. In some preferred embodiments, the JFSPC is characterized in c) and i) above. In some preferred embodiments, the JFSPC is characterized in d) and e) above. In some preferred embodiments, the JFSPC is characterized in d) and f) above. In some preferred embodiments, the JFSPC is characterized in d) and g) above. In some preferred embodiments, the JFSPC is characterized in d) and h) above. In some preferred embodiments, the JFSPC is characterized in d) and i) above. In some preferred embodiments, the JFSPC is characterized in e) and f) above. In some preferred embodiments, the JFSPC is characterized in e) and g) above. In some preferred embodiments, the JFSPC is characterized in e) and h) above. In some preferred embodiments, the JFSPC is characterized in e) and i) above. In some preferred embodiments, the JFSPC is characterized in f) and g) above. In some preferred embodiments, the JFSPC is characterized in f) and h) above. In some preferred embodiments, the JFSPC is characterized in f) and i) above. In some preferred embodiments, the JFSPC is characterized in g) and h) above. In some preferred embodiments, the JFSPC is characterized in g) and i) above. In some preferred embodiments, the JFSPC is characterized in h) and i) above. In some preferred embodiments, the JFSPC is characterized in a), b) and c) above. In some preferred embodiments, the JFSPC is characterized in a), b) and d) above. In some preferred embodiments, the JFSPC is characterized in a), b) and e) above. In some preferred embodiments, the JFSPC is characterized in In some preferred embodiments, the JFSPC is characterized in a) b) and f) above In some preferred embodiments the JFSPC is characterized in a), b) and g) above. In some preferred embodiments, the JFSPC is characterized in a), b) and h) above. In some preferred embodiments, the JFSPC is characterized in a), b) and i) above. In some preferred embodiments, the JFSPC is characterized in b), c) and d) above. In some preferred embodiments, the JFSPC is characterized in b), c) and e) above. In some preferred embodiments, the JFSPC is characterized in b), c) and f) above. In some preferred embodiments, the JFSPC is characterized in b), c) and g) above. In some preferred embodiments, the JFSPC is characterized in b), c), and h) above. In some preferred embodiments, the JFSPC is characterized in b), c) and i) above. In some preferred embodiments, the JFSPC is characterized in c), d) and e) above. In some preferred embodiments, the JFSPC is characterized in c), d) and f) above. In some preferred embodiments, the JFSPC is characterized in c), d) and g) above. In some preferred embodiments, the JFSPC is characterized in c), d) and h) above. In some preferred embodiments, the JFSPC is characterized in c), d) and i) above. In some preferred embodiments, the JFSPC is characterized in d), e) and f) above. In some preferred embodiments, the JFSPC is characterized in d), e) and g) above. In some preferred embodiments, the JFSPC is characterized in d), e) and h) above. In some preferred embodiments, the JFSPC is characterized in d), e) and i) above. In some preferred embodiments, the JFSPC is characterized in e), f) and g) above. In some preferred embodiments, the JFSPC is characterized in e), f) and h) above. In some preferred embodiments, the JFSPC is characterized in e), f) and i) above. In some preferred embodiments, the JFSPC is characterized in f), g) and h) above. In some preferred embodiments, the JFSPC is characterized in f), g) and i) above. In some preferred embodiments, the JFSPC is characterized in g), h) and i) above. In some preferred embodiments, the JFSPC is characterized in a), b), c) and d) above. In some preferred embodiments, the JFSPC is characterized in a), b), c) and e) above. In some preferred embodiments, the JFSPC is characterized in a), b), c) and f) above. In some preferred embodiments, the JFSPC is characterized in a), b), c) and g) above. In some preferred embodiments, the JFSPC is characterized in a), b), c) and h) above. In some preferred embodiments, the JFSPC is characterized in a), b), c) and i) above. In some preferred embodiments, the JFSPC is characterized in b), c), d) and e) above. In some preferred embodiments, the JFSPC is characterized in b), c), d) and f) above. In some preferred embodiments, the JFSPC is characterized in b), c), d) and g) above. In some preferred embodiments the JFSPC is characterized in b) c) d) and h) above In some preferred embodiments, the JFSPC is characterized in b), c), d) and i) above. In some preferred embodiments, the JFSPC is characterized in c), d), e) and f) above. In some preferred embodiments, the JFSPC is characterized in c), d), e) and g) above. In some preferred embodiments, the JFSPC is characterized in c), d), e) and h) above. In some preferred embodiments, the JFSPC is characterized in c), d), e) and i) above. In some preferred embodiments, the JFSPC is characterized in d), e), f) and g) above. In some preferred embodiments, the JFSPC is characterized in d), e), f) and h) above. In some preferred embodiments, the JFSPC is characterized in d), e), f) and i) above. In some preferred embodiments, the JFSPC is characterized in e), f), g) and h) above. In some preferred embodiments, the JFSPC is characterized in e), f), g) and i) above. In some preferred embodiments, the JFSPC is characterized in f), g), h) and i) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d) and e) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d) and f) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d) and g) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d) and h) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d) and i) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e) and f) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e) and g) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e) and h) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e) and i) above. In some preferred embodiments, the JFSPC is characterized in c), d), e), f) and g) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e) and h) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e) and i) above. In some preferred embodiments, the JFSPC is characterized in c), d), e), f) and g) above. In some preferred embodiments, the JFSPC is characterized in c), d), e), f) and h) above. In some preferred embodiments, the JFSPC is characterized in c), d), e), f) and i) above. In some preferred embodiments, the JFSPC is characterized in d), e), f), g) and h) above. In some preferred embodiments, the JFSPC is characterized in c), d), e), f) and i) above. In some preferred embodiments, the JFSPC is characterized in d), e), f), g) and h) above. In some preferred embodiments, the JFSPC is characterized in d), e), f), g) and i) above. In some preferred embodiments, the JFSPC is characterized in e), f), g), h) and i) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d), e) and f) above In some preferred embodiments the JFSPC is characterized in a) b) c) d) e) and g) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d), e) and h) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d), e) and i) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e), f) and g) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e), f) and h) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e), f) and i) above. In some preferred embodiments, the JFSPC is characterized in c), d), e), f), g) and h) above. In some preferred embodiments, the JFSPC is characterized in c), d), e), f), g) and i) above. In some preferred embodiments, the JFSPC is characterized in d), e), f), g), h) and i) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d), e), f) and g) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d), e), f) and h) above. In some preferred embodiments, the JFSPC is characterized in a), b), c), d), e), f) and i) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e), f), g) and h) above. In some preferred embodiments, the JFSPC is characterized in b), c), d), e), f), g) and i) above. In some preferred embodiments, the JFSPC is characterized in c), d), e), f), g), h) and i) above. In preferred embodiments, the jackfruit seed protein concentrates or compositions are utilized in food products. In some preferred embodiments, the food products comprise jackfruit seed protein concentrates or compositions at concentration of from 0.01% to 99.9% w/w of the food product, wherein w/w is weight of the iron-complexed phycocyanobilin compounds or composition divided by the total weight of the food product. In some preferred embodiments, the food products comprise 0.01% to 50% w/w of the jackfruit seed protein concentrates and compositions. In some preferred embodiments, the food products comprise 0.01% to 20% w/w of the jackfruit seed protein concentrates and compositions. In some preferred embodiments, the food products comprise 0.01% to 10% w/w of the jackfruit seed protein concentrates and compositions. In some preferred embodiments, the food products comprise 0.01% to 5% w/w of the jackfruit seed protein concentrates and compositions. In some preferred embodiments, the food products comprise 0.1% to 50% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 0.1% to 20% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 0.1% to 10% w/w of the jackfruit seed protein concentrates or compositions In some preferred embodiments the food products comprise 0.1% to 5% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 0.5% to 50% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 0.5% to 20% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 0.5% to 10% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 0.5% to 5% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 1.0% to 50% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 1.0% to 20% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 1.0% to 10% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products comprise 1.0% to 5% w/w of the jackfruit seed protein concentrates or compositions. In some preferred embodiments, the food products do not contain animal proteins or are free from animal proteins. In some embodiments, the food products additionally comprise one or more isolated, purified proteins. In some embodiments, about 0.1%, 0.2%, 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% or more of the protein component of a food product is comprised of the one or more additional isolated, purified proteins. For the purposes of this document, “purified protein” will refer to a preparation in which the cumulative abundance by mass of protein components other than the specified protein, which can be a single monomeric or multimeric protein species, is reduced by a factor of 2 or more, 3 or more, 5 or more, 10 or more, 20 or more, 50 or more, 100 or more or 1000 or more relative to the source material from which the specified protein was isolated. The additional protein in the food product can come from a variety or combination of sources. Non-animal sources can provide some or all of the protein in the food product. Non- animal sources can include vegetables, fruits, nuts, grains, algae, bacteria, or fungi. The protein can be isolated or concentrated from one or more of these sources. In some embodiments the food product is a meat replica comprising protein only obtained from non- animal sources In some embodiments, the one or more isolated, purified proteins are derived from non-animal sources. Non-limiting examples of non-animal sources include plants, fungi, bacteria, archaea, genetically modified organisms such as genetically modified bacteria or yeast, chemical or in vitro synthesis. In particular embodiments, the one or more isolated, purified proteins are derived from plant sources. Non-limiting examples of plant sources include grains such as, e.g., corn, maize, rice, wheat, barley, rye, triticale, teff, oilseeds including cottonseed, sunflower seed, safflower seed, rapeseed, leafy greens such as, e.g., lettuce, spinach, kale, collard greens, turnip greens, chard, mustard greens, dandelion greens, broccoli, cabbage, green matter not ordinarily consumed by humans, including biomass crops, including switchgrass, miscanthus, sorghum, other grasses, alfalfa, corn stover, green matter ordinarily discarded from harvested plants, sugar cane leaves, leaves of trees, root crops such as cassava, sweet potato, potato, carrots, beets, turnips, plants from the legume family, such as, e.g., clover, peas such as cowpeas, English peas, yellow peas, green peas, beans such as, e.g., soybeans, fava beans, lima beans, kidney beans, garbanzo beans, mung beans, pinto beans, lentils, lupins, mesquite, carob, soy, and peanuts, vetch (vicia), stylo (stylosanthes), arachis, indigofera, acacia, leucaena, cyamopsis, and sesbania. One of skill in the art will understand that proteins that can be isolated from any organism in the plant kingdom may be used in the present invention. Proteins that are abundant in plants can be isolated in large quantities from one or more source plants and thus are an economical choice for use in food products of the instant invention. Accordingly, in some embodiments, the one or more isolated proteins comprises an abundant protein found in high levels in a plant and capable of being isolated and purified in large quantities. In some embodiments, the abundant protein comprises about 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70% of the total protein content of the source plant. In some embodiments, the abundant protein comprises about 0.5-10%, about 5-40%, about 10-50%, about 20-60%, or about 30-70% of the total protein content of the source plant. In some embodiments, the abundant protein comprises about 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50% of the total weight of the dry matter of the source plant. In some embodiments, the abundant protein comprises about 0.5-5%, about 1-10%, about 5-20%, about 10-30%, about 15-40%, about 20-50% of the total weight of the dry matter of the source plant. In particular embodiments, the one or more isolated proteins comprises an abundant protein that is found in high levels in the leaves of plants In some embodiments the abundant protein comprises about 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80% of the total protein content of the leaves of the source plant. In some embodiments, the abundant protein comprises about 0.5-10%, about 5%-40%, about 10%-60%, about 20%-60%, or about 30-70% of the total protein content of the leaves of the source plant. In particular embodiments, the one or more isolated proteins comprise ribulose-1,5-bisphosphate carboxylase oxygenase (rubisco activase). Rubisco is a particularly useful protein for food products because of its high solubility and an amino acid composition with close to the optimum proportions of essential amino acids for human nutrition. In particular embodiments, the one or more isolated proteins comprise ribulose-15-bisphosphate carboxylase oxygenase activase (rubisco activase). In particular embodiments, the one or more isolated proteins comprise a vegetative storage protein (VSP). In some embodiments, the one or more isolated proteins include an abundant protein that is found in high levels in the seeds of plants. In some embodiments, the abundant protein comprises about 0.5%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85% or 90% or more of the total protein content of the seeds of the source plant. In some embodiments, the abundant protein comprises about 0.5-10%, about 5%-40%, about 10%-60%, about 20%-60%, or about 30-70% or >70% of the total protein content of the seeds of the source plant. Non-limiting examples of proteins found in high levels in the seeds of plants are seed storage proteins, e.g., albumins, glycinins, conglycinins, globulins, vicilins, conalbumin, gliadin, glutelin, gluten, glutenin, hordein, prolamin, phaseolin (protein), proteinoplast, secalin, triticeae gluten, zein, any seed storage protein, oleosins, caloleosins, steroleosins or other oil body proteins. In some embodiments, the protein component comprises the 8S globulin from Moong bean seeds, or the albumin or globulin fraction of pea seeds. These proteins provide examples of proteins with favorable properties for constructing meat replicas because of their ability to form gels with textures similar to animal muscle or fat tissue. Examples and embodiments of the one or more isolated, purified proteins are described herein. The list of potential candidates here is essentially open and may include Rubisco, any major seed storage proteins, proteins isolated from fungi, bacteria, archaea, viruses, or genetically engineered microorganisms, or synthesized in vitro. The proteins may be artificially designed to emulate physical properties of animal muscle tissue. The proteins may be artificially designed to emulate physical properties of animal muscle tissue. In some embodiments, one or more isolated purified proteins accounts for about 01% 02% 05% 1% 2% 3% 4% 5% 6% 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 99% or more of the protein component by weight. In some embodiments, the food products additionally comprise an added fat. In preferred embodiments, the added fat is from a source other than Spirulina. In preferred embodiments, the added fat is from a non-animal source. In some embodiments the fat content of the food product is 1%, 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, or 60% fat. In some embodiments, the fat component comprises a gel with droplets of fat suspended therein. In some embodiments, the gel is a soft, elastic gel comprising proteins and optionally carbohydrates. In particular embodiments, the proteins used in the gel are plant or microbial proteins. In some embodiments, the proteins used in the fat component might include Rubisco, any major seed storage proteins, proteins isolated from fungi, bacteria, archaea, viruses, or genetically engineered microorganisms, or synthesized in vitro. The fat droplets used in some embodiments of the present invention can be from a variety of sources. In some embodiments, the sources are non-animal sources. In particular embodiments, the sources are plant sources. Non-limiting examples of oils include corn oil, olive oil, soy oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flax seed oil, algal oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, oils produced by bacteria, algae, archaea or fungi or genetically engineered bacteria, algae, archaea or fungi, triglycerides, monoglycerides, diglycerides, sphingosides, glycolipids, lecithin, lysolecithin, phophatidic acids, lysophosphatidic acids, oleic acid, palmitoleic acid, palmitic acid, myristic acid, lauric acid, myristoleic acid, caproic acid, capric acid, caprylic acid, pelargonic acid, undecanoic acid, linoleic acid, 20:1 eicosanoic acid, arachidonic acid, eicosapentanoic acid, docosohexanoic acid, 18:2 conjugated linoleic acid, conjugated oleic acid, or esters of: oleic acid, palmitoleic acid, palmitic acid, myristic acid, lauric acid, myristoleic acid, caproic acid, capric acid, caprylic acid, pelargonic acid, undecanoic acid, linoleic acid, 20:1 eicosanoic acid, arachidonic acid, eicosapentanoic acid, docosohexanoic acid, 18:2 conjugated linoleic acid, or conjugated oleic acid, or glycerol esters of oleic acid, palmitoleic acid, palmitic acid, myristic acid, lauric acid, myristoleic acid, caproic acid, capric acid, caprylic acid, pelargonic acid, undecanoic acid, linoleic acid, 20:1 eicosanoic acid, arachidonic acid, eicosapentanoic acid, docosohexanoic acid, 18:2 conjugated linoleic acid, or conjugated oleic acid, or triglyceride derivatives of oleic acid, palmitoleic acid, palmitic acid, myristic acid lauric acid myristoleic acid caproic acid capric acid caprylic acid pelargonic acid, undecanoic acid, linoleic acid, 20:1 eicosanoic acid, arachidonic acid, eicosapentanoic acid, docosohexanoic acid, 18:2 conjugated linoleic acid, or conjugated oleic acid. In some embodiments, fat droplets are derived from pulp or seed oil. In other embodiments, the source may be yeast or mold. For instance, in one embodiment the fat droplets comprise triglycerides derived from Mortierella isabellina. In some embodiments, the fat component comprises a protein component comprising one or more isolated, purified proteins. The purified proteins contribute to the taste and texture of the food product. In some embodiments purified proteins can stabilize emulsified fats. In some embodiments the purified proteins can form gels upon denaturation or enzymatic crosslinking, which replicate the appearance and texture of animal fat. Examples and embodiments of the one or more isolated, purified proteins are described herein. In particular embodiments, the one or more isolated proteins comprise a protein isolated from the legume family of plants. Non-limiting examples of legume plants are described herein, although variations with other legumes are possible. In some embodiments, the legume plant is a pea plant. In some embodiments the isolated purified proteins stabilize emulsions. In some embodiments the isolated purified proteins form gels upon crosslinking or enzymatic crosslinking. In some embodiments, the isolated, purified proteins comprise seed storage proteins. In some embodiments, the isolated, purified proteins comprise albumin. In some embodiments, the isolated, purified proteins comprise globulin. In a particular embodiment, the isolated, purified protein is a purified pea albumin protein. In another particular embodiment, the isolated, purified protein is a purified pea globulin protein. In another particular embodiment the isolate purified protein is a Moong bean 8S globulin. In another particular embodiment, the isolated, purified protein is an oleosin. In another particular embodiment, the isolated, purified protein is a caloleosin. In another particular embodiment, the isolated, purified protein is Rubisco. In some embodiments, the protein component comprises about 0.1%, 0.5%, 1%, 2%, 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90% or more of the fat component by dry weight or total weight. In some embodiments, the protein component comprises about 0.1-5%, about 0.5-10%, about 1-20%, about 5-30%, about 10-50%, about 20-70%, or about 30-90% or more of the fat component by dry weight or total weight. In some embodiments, the protein component comprises a solution containing one or more isolated, purified proteins. In some embodiments, the fat component comprises cross-linking enzymes that catalyze reactions leading to covalent crosslinks between proteins. Cross-linking enzymes can be used to create or stabilize the desired structure and texture of the adipose tissue component to mimic the desired texture of an equivalent desired animal fat. Non-limiting examples of cross-linking enzymes include, e.g., transglutaminase, lysyl oxidases, or other amine oxidases (e.g. Pichia pastoris lysyl oxidase). In some embodiments, the cross-linking enzymes are isolated and purified from a non-animal source, examples and embodiments of which are described herein. In some embodiments, the fat component comprises at least 0.0001%, or at least 0.001%, or at least 0.01%, or at least 0.1%, or at least 1% (wt/vol) of a cross-linking enzyme. In particular embodiments, the cross-linking enzyme is transglutaminase. In some embodiments, the fat component is assembled to approximate the organization adipose tissue in meat. In some embodiments some or all of the components of the fat component are suspended in a gel. In various embodiments the gel can be a proteinaceous gel, a hydrogel, an organogel, or a xerogel. In some embodiments, the gel can be thickened to a desired consistency using an agent based on polysaccharides or proteins. For example fecula, arrowroot, cornstarch, katakuri starch, potato starch, sago, tapioca, alginin, guar gum, locust bean gum, xanthan gum, collagen, egg whites, furcellaran, gelatin, agar, carrageenan, cellulose, methylcellulose, hydroxymethylcellulose, acadia gum, konjac, starch, pectin, amylopectin or proteins derived from legumes, grains, nuts, other seeds, leaves, algae, bacteria, of fungi can be used alone or in combination to thicken the gel, forming an architecture or structure for the food product. In some embodiments, the fat component is an emulsion comprising a solution of one or more proteins and one or more fats suspended therein as droplets. In some embodiments, the emulsion is stabilized by one or more cross-linking enzymes into a gel. In more particular embodiments, the one or more proteins in solution are isolated, purified proteins. In yet more particular embodiments, the isolated, purified proteins comprise a purified pea albumin enriched fraction. In other more particular embodiments, the isolated, purified proteins comprise a purified pea globulin enriched fraction. In other more particular embodiments, the isolated, purified proteins comprise a purified Moong bean 8S globulin enriched fraction. In yet more particular embodiments, the isolated, purified proteins comprise a Rubisco enriched fraction. In other particular embodiments, the one or more fats are derived from plant-based oils. In more particular embodiments, the one or more fats are derived from one or more of: corn oil, olive oil, soy oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flax seed oil, algal oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, oils produced by bacteria, algae, archaea or fungi or genetically engineered bacteria algae archaea or fungi triglycerides monoglycerides diglycerides sphingosides glycolipids, lecithin, lysolecithin, phophatidic acids, lysophosphatidic acids, oleic acid, palmitoleic acid, palmitic acid, myristic acid, lauric acid, myristoleic acid, caproic acid, capric acid, caprylic acid, pelargonic acid, undecanoic acid, linoleic acid, 20:1 eicosanoic acid, arachidonic acid, eicosapentanoic acid, docosohexanoic acid, 18:2 conjugated linoleic acid, conjugated oleic acid, or esters of: oleic acid, palmitoleic acid, palmitic acid, myristic acid, lauric acid, myristoleic acid, caproic acid, capric acid, caprylic acid, pelargonic acid, undecanoic acid, linoleic acid, 20:1 eicosanoic acid, arachidonic acid, eicosapentanoic acid, docosohexanoic acid, 18:2 conjugated linoleic acid, or conjugated oleic acid, or glycerol esters of oleic acid, palmitoleic acid, palmitic acid, myristic acid, lauric acid, myristoleic acid, caproic acid, capric acid, caprylic acid, pelargonic acid, undecanoic acid, linoleic acid, 20:1 eicosanoic acid, arachidonic acid, eicosapentanoic acid, docosohexanoic acid, 18:2 conjugated linoleic acid, or conjugated oleic acid, or triglyceride derivatives of oleic acid, palmitoleic acid, palmitic acid, myristic acid, lauric acid, myristoleic acid, caproic acid, capric acid, caprylic acid, pelargonic acid, undecanoic acid, linoleic acid, 20:1 eicosanoic acid, arachidonic acid, eicosapentanoic acid, docosohexanoic acid, 18:2 conjugated linoleic acid, or conjugated oleic acid. In yet even more particular embodiments, the one or more fats is a rice bran oil. In another particular embodiment, the one or more fats is a canola oil. In other particular embodiments, the cross-linking enzyme is transglutaminase, lysyl oxidase, or other amine oxidase. In yet even more particular embodiments, the cross-linking enzyme is transglutaminase. In particular embodiments, the fat component is a high fat emulsion comprising a protein solution of purified pea albumin emulsified with 40-80% rice bran oil, stabilized with 0.5-5% (wt/vol) transglutaminase into a gel. In particular embodiments, the fat component is a high fat emulsion comprising a protein solution of partially-purified moong bean 8S globulin emulsified with 40-80% rice bran oil, stabilized with 0.5-5% (wt/vol) transglutaminase into a gel. In particular embodiments, the fat component is a high fat emulsion comprising a protein solution of partially-purified moong bean 8S globulin emulsified with 40-80% canola oil, stabilized with 0.5-5% (wt/vol) transglutaminase into a gel. In particular embodiments, the fat component is a high fat emulsion comprising a protein solution of purified pea albumin emulsified with 40-80% rice bran oil, stabilized with 0.0001- 1% (wt/vol) transglutaminase into a gel. In particular embodiments, the fat component is a high fat emulsion comprising a protein solution of partially-purified moong bean 8S globulin emulsified with 40-80% rice bran oil, stabilized with 0.0001-1% (wt/vol) transglutaminase into a gel. In particular embodiments, the fat component is a high fat emulsion comprising a protein solution of partially-purified moong bean 8S globulin emulsified with 40-80% canola oil, stabilized with 0.0001-1% (wt/vol) transglutaminase into a gel. In some embodiments some or all of the components of the food product are suspended in a gel. In various embodiments the gel can be a hydrogel, an organogel, or a xerogel, The gel can be made thick using an agent based on polysaccharides or proteins. For example fecula, arrowroot, cornstarch, katakuri starch, potato starch, sago, tapioca, alginin, guar gum, locust bean gum, xanthan gum, collagen, egg whites, furcellaran, gelatin, agar, carrageenan, cellulose, methylcellulose, hydroxymethylcellulose, acadia gum, konjac, starch, pectin, amylopectin or proteins derived from legumes, grains, nuts, other seeds, leaves, algae, bacteria, of fungi can be used alone or in combination to thicken the gel, forming an architecture or structure for the food product. Enzymes that catalyze reactions leading to covalent crosslinks between proteins can also be used alone or in combination to form an architecture or structure for the food product. For example, transclutaminase, lysyl oxidases, or other amine oxidases (e.g. Pichia pastoris lysyl oxidase (PPLO)) can be used alone or in combination to form an architecture or structure for the food product. In some embodiments multiple gels with different components are combined to form the food product. For example, a gel containing a plant-based protein can be associated with a gel containing a plant-based fat. In some embodiments fibers or stings of proteins are oriented parallel to one another and then held in place by the application of a gel containing plant-based fats. In some embodiments the food product composition contains no animal protein, comprising between 10-30% protein, between 5-80% water, between 5-70% fat, and further comprising one or more isolated purified proteins. In particular embodiments, the food product compositions comprise transglutaminase. In some embodiments the food product contains components to replicate the components of meat. The main component of meat is typically skeletal muscle. Skeletal muscle typically consists of roughly 75 percent water, 19 percent protein, 2.5 percent intramuscular fat, 1.2 percent carbohydrates and 2.3 percent other soluble non-protein substances. These include organic acids, sulfur compounds, nitrogenous compounds, such as amino acids and nucleotides, and inorganic substances such as minerals. Accordingly, some embodiments of the present invention provide for replicating approximations of this composition for the food product. For example, in some embodiments the food product is a plant-based meat replica can comprise roughly 75% water, 19% protein, 2.5% fat, 1.2% carbohydrates; and 2.3 percent other soluble non-protein substances. In some embodiments the food product is a plant-based meat replica comprising between 60-90% water 10-30% protein, 1-20% fat, 0.1-5% carbohydrates; and 1-10 percent other soluble non-protein substances. In some embodiments the food product is a plant-based meat replica comprising between 60-90% water, 5-10% protein, 1-20% fat, 0.1-5% carbohydrates; and 1-10 percent other soluble non-protein substances. In some embodiments the food product is a plant-based meat replica comprising between 0-50% water, 5-30% protein, 20-80%% fat, 0.1-5% carbohydrates; and 1-10 percent other soluble non-protein substances. In some embodiments, the replica contains between 0.01% and 5% by weight of a heme protein. In some embodiments, the replica contains between 0.01% and 5% by weight of leghemoglobin. Some meat also contains myoglobin, a heme protein, which accounts for most of the red color and iron content of some meat. In some embodiments, the replica contains between 0.01% and 5% by weight of a heme protein. In some embodiments, the replica contains between 0.01% and 5% by weight of leghemoglobin. It is understood that these percentages can vary in meat and the meat replicas can be produced to approximate the natural variation in meat. Additionally, in some instances, the present invention provides for improved meat replicas, which comprise these components in typically unnatural percentages. EXAMPLES Example 1 Feedstock. Raw jackfruit was sliced, and the seeds were manually separated from the flesh. A total amount of 210 JFSs were then collected, washed with tap water, blended and left to dry overnight on a tray at 50 °C. JFS moisture content decreased from 39.3% to 2.9% with a total dry mass of 374.4 g. The JFS blend was then ground in a coffee grinder to yield a white flour. Compositional Analysis. JFS samples were defatted for 24 h by extraction with hexane in a Soxhlet system. The defatted samples were then stored for the protein extraction tests. Part of the defatted biomass was then extracted with water for 24 h in Soxhlet system. The water-extracted sample was subjected to compositional analysis and ash quantification. Structural carbohydrates — glucan, xylan, arabinan — and acid-soluble and insoluble lignin were quantified according to the National Renewable Energy Laboratory (NREL) standard methods for lignocellulosic feedstocks (Sluiter et al., 2016). Ash quantification was performed by direct ashing the biomass at 575 °C in a muffle oven for at least 3 h according to Sluiter et al. (2008). Moisture content of the samples was determined by the mass difference between the wet and dry sample after drying overnight at 105 °C in a convection oven Starch content was determined using a modified version of the Megazyme Rapid Total Starch Assay procedure (Megazyme, 2020), in which released glucose was determined by HPLC rather than spectrophotometry. Out of the several Megazyme procedures, this was found to be most suitable for the feedstocks used. A Megazyme Total Starch Assay kit was purchased, containing the enzymes used in this procedure: thermostable α-amylase (2500 U/m) and amyloglucosidase (3,300 U/mL). In this process, a large excess of both enzymes were added to fully hydrolyse any starch present in the samples. The resulting glucose quantified, allowing the original starch content to be determined. Protein extraction. Protein isolates from JSF were prepared using the alkaline extraction and isoelectric precipitation technique as described by Zhang et al. (2019) with some modifications. Approximately 5 g of defatted JFS (in dry basis) were mixed in a beaker with NaOH or MEA 0.05 mol/L solutions to a total mixture mass of 50 g (10 wt% solids loading). The dispersion was stirred for 1 h at room temperature and then centrifuged at 5000×g for 15 min. The protein from the supernatants was isoelectrically precipitated at pH 4.3 with 1 M HCl and kept at 4 °C for 1 h. The precipitate was collected by centrifugation at 5000g for 15 min and washed with deionized water. SDS-PAGE was performed on a discontinuous buffered system according to the method of Ma et al. (2018) and Zhang et al. (2019), using 12% separating gel and 4% stacking gel. The protein isolates (2-5 mg/mL) were solubilized in sample buffer. Then, the samples were heated in a boiling water bath for 10 min before electrophoresis. Each lane of the gel was loaded with 10μL of sample. After running for 15 min at a constant voltage of 80V, the samples were run for 43 min at a constant voltage of 120 V. The gel was stained for 2h with 0.05% Coomassie blue (R-250) and was then destained in decoloring solution (methanol/acetic acid/water, 50:75:875) for 8 h. Compositional analysis of JFS. The chemical composition of JFS is shown in Fig.1. Nearly 80 wt% of the biomass is composed of proteins and starch, which shows an interesting potential for JFS utilization. The protein content was 11.41 wt%, slightly lower than the values obtained by Ocloo et al. (2010), 13.5%. and Singh et al. (1991), 17.2 wt%. The lignin content is also low (8 wt%), which also reduces the cost of overall biomass processing related with lignin downstream. The results obtained are in agreement with JFSs chemical composition reported by Ocloo et al. (2010), however, the carbohydrate content found in this work was lower (71.7% versus 79.3%), which might be due to differences related with variabilities in harvest season and JF variety. Protein extraction. The extraction yields for the protein isolates were shown in Table 3. Sodium hydroxide extraction was twice as higher than monoethanolamine, which indicates that the strength of the base (as also shown by the pH of the medium) is a key factor for protein extraction. It is important to address that although NaOH extraction had a higher yield, the samples presented lower purity (nearly 60% against 73%) and they were also subjected to higher variability (8.5% compared to 0.7%) than that of MEA. Sample variability might be due to variations mass transfer in the extraction system possibly related with particle size/agglomeration. The fact that MEA extraction produces a purer protein isolate may implicate a cheaper downstream of the proteins. Table 3. Results obtained from the protein extraction tests.

SDS-page. The protein profiles of JFS proteins were determined by SDS-PAGE. There were no significant differences between proteins extracted by either NaOH or MEA, which indicates both alkalis presented similar mechanism of action. The major high intensity bands are observed at approximately 26, 20, 14 and 12 kDa in a similar result obtained by Zhang et al. (2019). Resendiz-Vazquez et al. (2017) reported that the electrophoretic profile of JSF proteins included seven main bands, and their molecular weight distribution consisted of bands at 26.82, 22.94, 21.52, 18.05, 15.85, 10.98 and 6.08 kDa. Conclusions. The compositional analysis of JFS revealed that up to 80 wt% of the seeds are composed of protein and starch, which could result in a potential process for protein extraction followed by starch purification/production. The alkaline extraction with NaOH reached nearly 56% and provided a brownish protein isolate with 60% of purity. Whereas MEA extraction had nearly half of the extraction yield, 29% but it also produced a much purer protein isolate (73% purity) which suggests a more selective extraction might has taken place. The SDS-page analysis showed good agreement with results in the literature and also confirmed the isolated proteins did not undergo degradation into small oligopeptides REFERENCES FOR EXAMPLE 1: Bernardino-Nicanor, A., Bravo-Delgado, C.H., Vivar-Vera, G., et al., 2014. Preparation, composition, and functional properties of a protein isolate from a defatted mamey sapote (Pouteria sapota) seed meal. Cyta-Journal of Food, 12, 176–182. doi:10.1080/ 19476337.2013.81067 4 Du, L., Arauzo, P.J., Meza Zavala, et al., Towards the Properties of Different Biomass-Derived Proteins via Various Extraction Methods, Molecules.25 2020). Haque M. A., Akter, F., Rahman, H., Baqui, M. A., 2020. Jackfruit Seeds Protein Isolate by Spray Drying Method: The Functional and Physicochemical Characteristics, Food and Nutrition Sciences, 11(5), 355-374. Hou, F., Ding, W., Qu, W., et al. He, H. Ma, Alkali solution extraction of rice residue protein isolates: Influence of alkali concentration on protein functional, structural properties and lysinoalanine formation, Food Chem.218 (2017) 207–215. Jangchud, A., Chinnan, M.S., Properties of Peanut Protein Film: Sorption Isotherm and Plasticizer Effect, LWT - Food Sci. Technol.32 (1999) 89–4. Kabir S. The isolation and characterisation of jacalin [Artocarpus heterophyllus (jackfruit) lectin] based on its charge properties. Int J Biochem Cell Biol. 1995 Feb;27(2):147-56. doi: 10.1016/1357-2725(94)00071-i. PMID: 767783. Kumar, S., Appukuttan, P.S. and Debkumar Basu. (1982). a-D-Galactose-specific lectin from jack fruit (Artocarpusintegra) seed. Journal of Biosciences, 4(3), 257-261 Madrigal-Aldana, D.L., Tovar-Gomez, B., Mata-Montes de Oca, et al., 2011. Isolation and characterization of Mexican jackfruit (Artocarpus heterophyllus L) seeds atrch in two mature stages. Starch/Starke 63, 364–372. Megazyme, 2020 TOTAL STARCH ASSAY PROCEDURE (AMYLOGLUCOSIDASE/ α- AMYLASE METHOD).; 2020. www.megazyme.com. Madruga, M.S., Medeiros De Albuquerque, F.S., Alves Silva, et al., 2014. Chemical, morphological and functional properties of Brazilian jackfruit (Artocarpus heterophyllus L.) seeds starch. Food Chemistry, 143, 440–445. Nakasu, P.Y.S., Clarke, C.J., Rabelo, S.C., et al., Interplay of Acid–Base Ratio and Recycling on the Pretreatment Performance of the Protic Ionic Liquid Monoethanolammonium Acetate, ACS Sustain. Chem. Eng. 8 (2020) 7952–7961. https://doi.org/10.1021/acssuschemeng.0c01311. Omale, J., & Friday, E. (2010). Phytochemical composition, bioactivity and wound healing potential of Euphorbia Heterophylla (Euphorbiaceae) leaf extract. International. Journal of Pharmaceutical and Biomedical Research, 1, 54–63. Ocloo, F.C.K., Bansa, D., Boatin, R., Adom, T., Agbemavor, W.S., 2010. Physico-chemical, functional and pasting characteristics of flour produced from Jackfruits (Artocarpus heterophyllus) seeds. Agri. Biology J. North Am.1, 903–908. Resendiz-Vazquez, J. A., Ulloa, J. A., Urias-Silvas, J. E., Bautista-Rosales, P. U., Ramirez- Ramirez, J. C., Rosas-Ulloa, P., et al. (2017). Effect of high-intensity ultrasound on the technofunctional properties and structure of jackfruit (Artocarpus heterophyllus) seed protein isolate. Ultrasonics Sonochemistry, 37, 436–444. Seow, C.C., Shanmugan, G., 1992. Storage stability of canned jackfruit (Artocarpus heterophyllus) juice at tropical temperature. J. Food Sci. Technol.29, 371–374. Singh, A., Kumar, S., Singh, I.S., 1991. Functional properties of jackfruit seed flour. LWT- Food Sci. Technol.24, 373–374. Sluiter, J.B., Chum, H., Gomes, A.C., et al., Evaluation of Brazilian sugarcane bagasse characterization: An interlaboratory comparison study, J. AOAC Int. 99 (2016) 579–585. https://doi.org/10.5740/jaoacint.15-0063. Swami, S.B., Thakor, N.J., Haldankar, P.M., & Kalse, S.B. (2012). Jackfruit and its many functional components as related to human health: A review. Comprehensive Reviews in Food Science and Food Safety, 11, 565–576. doi:10.1111/j.1541-4337.2012.00210.x Vazquez, J.A., Urías-Silvas, J.E., Ulloa, J. Arm, O., P.U. Bautista-Rosales, J.C. Ramírez- Ramírez, Effect of Ultrasound-assisted Enzymolysis on Jackfruit (Artocarpus heterophyllus) Seed Proteins: Structural Characteristics, Technofunctional Properties and the Correlation to Enzymolysis, J. Food Process. Technol.10 (2019) 1–11. Example 2 1. Feedstock JFS flour was sourced from a commercial supplier. The flour was defatted to remove lipids by Soxhlet extraction. The extraction of lipids, also known as defatting, has been demonstrated to improve protein extraction yields from various plant biomass (e.g. soybean, canola) (Alibhai et al., 2006 [27]). Cellulose thimbles filled with 4g of flour was extracted for 20-24 hours with 150 ml of cyclohexane using the Soxhlet system. After extraction, the thimbles were left to air dry overnight. The JFS flour was then stored in an air-tight container at room temperature (20°C), away from direct sunlight. 2. Compositional Analysis The composition of the defatted JFS flour was determined using the same methods as in Phase 1 of this study. Firstly, the flour was subjected to water extraction for 20-24 hours using the Soxhlet system. The water-extracted sample was then subjected to compositional analysis and ash quantification. Structural carbohydrates — glucan, xylan, arabinan — and acid-soluble and insoluble lignin were quantified according to the National Renewable Energy Laboratory (NREL) standard methods for lignocellulosic feedstocks [28]. Ash quantification was performed by directly ashing the sample at 575 °C in a muffle oven, following the heating profile described by Sluiter et al. (2008) [29]. The moisture content of the samples was determined by the mass difference between the wet and dry sample after drying at 105°C in a convection oven for at least six hours. Starch content was determined using a modified version of the Megazyme Rapid Total Starch Assay procedure [30], in which released glucose was determined by HPLC rather than spectrophotometry. Out of the several Megazyme procedures, this was found to be most suitable for the feedstocks used. A Megazyme Total Starch Assay kit was purchased, containing the enzymes used in this procedure: thermostable α-amylase (2500 U/m) and amyloglucosidase (3,300 U/mL). In this process, a large excess of both enzymes was added to fully hydrolyse any starch present in the samples. The resulting glucose was quantified, allowing the original starch content to be determined. 3. Protein Extraction Protein isolates from defatted JFS flour were prepared using the alkaline extraction and isoelectric precipitation technique as described by Zhang et al. (2019)[31], with some modifications. Firstly, a design of experiments was followed to optimise the key conditions of the protein extraction, using both choline hydroxide (ChOH) and sodium hydroxide (NaOH) (Step 1). Then a range of dilute concentrations of both ChOH and NaOH solutions were tested including an additional 2-step sequential extraction (Step 2). This was repeated with monoethanolamine (MEA) (Step 3). Unfatted (raw) JFS flour was also trialled (Step 4) before a final screening of the alkali solution concentration (Step 5). Finally, a combination of MEA and ChOH was also tested (Step 6). Step 1: Initial protein extraction optimisation Approximately 2g of defatted JFS flour (dry basis) was added to a beaker with either ChOH or NaOH solution to achieve a 10 wt% solids loading. The total mixture of mass 20g was fully dispersed by continuous stirring at 600 RPM. A design of experiments using the Box-Behnken method was carried out to test the following conditions of the protein extraction: alkali concentration (mol/L), extraction time (hours) and temperature (°C). Table 4 summarises the extraction conditions that were tested with both ChOH and NaOH, which resulted in 11 assays each, including triplicates of the centre point conditions (50°C, 2 hours and 0.55mol/L). Table 4. Design of experiments for protein extraction optimisation

Upon protein extraction, the extract slurry was centrifuged at 5000 × g for 30 minutes. The supernatant was then decanted from the JFS solids residue. The protein in the supernatants was isoelectrically precipitated at pH 4.3 by the addition of hydrochloric acid (HCl). The precipitate was collected by centrifugation at 5000 × g for 15 minutes and washed three times with deionized water. The solids residues were also washed three times with deionized water and then freeze dried along with the protein precipitates. Step 2: Dilute alkali protein extraction with sequential extractions As in Step 1, approximately 2g of defatted JFS flour (dry basis) was added to a beaker with either ChOH or NaOH solution, but at a 0.05, 0.1 or 0.2 mol/L concentration to achieve a 10 wt% solids loading. The total mixture of mass 20g was fully dispersed by continuous stirring at 600 RPM for 1 hour at room temperature (20°C). Upon protein extraction, the extract slurry was centrifuged at 5000 × g for 30 minutes. The supernatant was then decanted from the JFS solids residue. The solids residue was then subjected to sequential extraction twice for 30 minutes each at room temperature by continuous stirring (600 RPM). The supernatant was collected after each sequential extraction by centrifugation (at 5000 × g for 30 minutes) and combined with the first supernatant. The protein in the combined supernatants was isoelectrically precipitated, washed and freeze dried as in Step 1. Similarly, the solids residues were also washed and freeze dried. Step 3: Dilute MEA protein extraction with sequential extractions Step 2 was repeated with MEA. Approximately 2 g of defatted JFS flour (dry basis) was added to a beaker MEA solution of either 0.05, 0.1 or 0.2 mol/L to achieve a 10 wt% solids loading. The total mixture of mass 20g was fully dispersed by continuous stirring at 600 RPM for 1 hour at room temperature (20°C). Sequential extractions, protein isoelectric precipitation, protein and solid residue washing then drying was carried out as in Step 2. Step 4: Unfatted (raw) protein extraction Approximately 2 g of unfatted (raw) JFS flour (dry basis) was added to a beaker with 0.1 mol/L NaOH solution to achieve a 10 wt% solids loading. The total mixture of mass 20g was fully dispersed by continuous stirring at 600 RPM. As in Step 1, upon protein extraction, the extract slurry was centrifuged at 500 × g for 30 minutes. The supernatant was then decanted from the JFS solids residue. The protein in the combined supernatants was isoelectrically precipitated, washed and freeze dried as in Step 1. Similarly, the solids residues were also washed and freeze dried. Step 5: Dilute alkali protein extraction screening As in Step 1, approximately 2g of defatted JFS flour (dry basis) was added to a beaker with either ChOH or NaOH solution, this time at a 0.04, 0.03, 0.02 or 0.01 mol/L concentration to achieve a 10 wt% solids loading. The total mixture of mass 20g was fully dispersed by continuous stirring at 600 RPM for 1 hour at room temperature (20°C). Sequential extractions, protein isoelectric precipitation, protein and solid residue washing then drying was carried out as in Step 2. Step 6: Combined alkali protein extraction MEA and ChOH was combined to make a 0.05 mol/L solution. Approximately 2 g of defatted JFS flour (dry basis) was added to a beaker with this solution, to achieve a 10 wt% solids loading. The total mixture of mass 20g was fully dispersed by continuous stirring at 600 RPM for 1 hour at room temperature (20°C). Sequential extractions, protein isoelectric precipitation, protein and solid residue washing then drying was carried out as in Step 2. 4. Protein Extraction Scale Up In order to conduct an amino acid profiling of the JFS protein isolates, and investigate their functional and organoleptic properties, a scale up of the protein extraction procedure was carried out to mass produce the protein precipitate. Extractions were carried out in batches of 4, where each extraction used approx.28.9 g of JFS flour (dry basis) with a 10 wt% solids loading. The total mixture of mass 289g was fully dispersed by continuous stirring at 600 RPM for at least 1 hour at room temperature (20°C). Upon protein extraction, the extract slurry was centrifuged at 5000 x g for 30 minutes. The supernatant was decanted from the JFS solids residue, which was then discarded. The total supernatant from each batch was combined into one large container and isoelectrically precipitated at pH 4.3 by the addition of hydrochloric acid (HCl). The protein precipitate was collected by centrifugation in 500ml conical flasks at 5000 × g for 15 minutes. Afterwards, the precipitate was washed three times with deionized water before freeze drying. 5. Amino Acid Profiling Protein precipitate samples of approx.2g were sent to Sciantec Analytical Services (UK) for amino acid profiling. Samples were analysed for the following amino acids: cystine (Cys/C), aspartic acid, methionine (Met/M), threonine (Thr/T), serine (Ser/S), glutamic acid (Glu/E), glycine (Gly/G), alanine (Ala/A), valine (Val/V), iso-leucine (Ile/I), leucine (Leu/L), tyrosine (Tyr/Y), phenylalanine (Phe/F), histidine (His/H), lysine (Lys/K), arginine (Arg/gR, proline (Pro/P), and tryptophan (Trp). 5.1. Bulk density The bulk density determination protocol followed Haque et al., (2020). Five (5.0) g of JSPCs was put into a 25 mL measuring cylinder. The initial weight and the initial volume of the sample were recorded. The JSPCs powder was then poured into a cylinder and tapped continuously until a constant level was obtained. Again, the weight and volume of the sample were recorded. The final weight and volume of the sample were recorded from these differences. The bulk density (g/mL) was calculated as the weight of powder (g) divided by the volume of powder (mL) according to the Equation 1.

5.2 Water holding capacity The Water Holding Capacity (WHC) was measured by Haque et al., (2020) [32] with a slight modification. A 1-gram sample was dispersed in 10 g distilled water. The contents were mixed for 30 seconds every 10 minutes using a glass rod, and after seven mixings were centrifuged at 2000 × g for 15 minutes. The supernatant was carefully decanted, then the tube was inverted and drained for 15 minutes and finally weighed. The water absorbed was expressed as the percentage increase of sample weight. 5.3 Oil holding capacity The Oil Holding Capacity (OHC) of JSPCs was determined following a similar method for WHC, where rapeseed oil was used as a suspension medium instead of water. 5.4 Protein solubility To determine the protein solubility samples of protein isolate were suspended in water at different pH values (3–10) using the method described by Wang and Kinsella (1976) [33]. These solutions were then centrifuged at 3050 × g for 10 minutes, and the supernatants were analysed for protein using the Bradford method [34]. 5.5 Emulsion characterisation A modified version of the method described by Ulloa et al. (2017) [35]was used to determine the Emulsion Activity (EA) and the emulsion stability of the isolate. Three suspensions were prepared by dissolving 1 g of protein isolate in 30 ml of pH 4, 7 or 10 phosphate-citrate buffer. Then, 30 ml of rapeseed oil was added to each suspension. Each mixture was stirred in a blender for 1.5 minutes and centrifuged at 1190 × g for 5 min. The volume of the emulsion layer was recorded. The EA was calculated as follows:

The EA was estimated based on separated cream following the Equation 2. Emulsion stability at different pHs (4. 7 and 10) was determined according to the method of Pearce and Kinsella, (1978). The prepared emulsions were transferred into test tubes and held at 70 °C in a water bath for 45 minutes. Then the tubes were allowed to stand at room temperature for 3 hours. Percent stability was calculated from the height of the remaining emulsified layer after experimental time to that of the original emulsified layer, according to Equation 3:

5.6 Foaming properties Foaming capacity and stability of JSPCs at different pH (4.7 and 10) were determined according to the method described by Haque et al., (2020) [32]. The protein samples (0.5 g) were kept into 50 mL plastic containers and diluted with 50 mL of buffered solutions (pH 4, 7 and 10). The suspensions were mixed thoroughly using magnetic stirrer and finally homogenized in a blender for 1.5 min. The volume of the produced foam in each beaker was measured by measuring cylinder within no later than 30 seconds. The increment of foam volume was estimated following Equation 4 and expressed as percent foam capacity. The foam stability of JSPI was calculated by Equation 5.

5.7 Gelation characteristics The gelation capacity of JSPCs was determined according to the method followed by Haque et al., (2020) [32] with a slight modification. A range of sample suspensions from 4% to 20% (w/v) concentrations was prepared into two different solvents; distilled water and 1.0 mol/L NaCl solution. The test tubes containing these suspensions were then heated for 1 hour in a boiling water bath and followed by a rapid cooling under cold water tap. The tubes were further cooled for 2 hours at 4˚C. The least gelation concentration (LGC) was determined as the minimum concentration required to form a self-supporting gel when the sample did not fall or slip from the inverted test tube. Results and discussion 1. Compositional analysis The protein content of the flours (Table 5) was consistent across the different samples and did not vary much, which shows that there is little protein content variability across the samples. The overall protein content values were lower than the ones obtained by Ocloo et al. (2010)[36] , 13.5%. and Singh et al. (1991)[37] , 17.2 wt%. Amadi et al. (2018)[38], on the other hand, reported lower protein content in JFSs, 10.09%. Table 5. Protein content of the JFS samples.

The compositional analysis of the JFS flours is shown in Table 6. Overall, there were no major differences between the two samples, except for the higher lignin content in the Phase I sample which may be related with the sample handling. It could be possible that a higher amount of residual lignin was due to the presence of seed coats, which are more fibrous. Table 6. Compositional analysis of the JFS flours.

2. Optimisation of the protein extraction Protein yield and purity values for the optimisation experiments are shown in Fig. 2. Extraction time did not impact on the yield or protein purity. Temperature had a moderate effect on such parameters with the highest yield and purity values at low temperature. The alkali concentration seemed to affect both outcome variables. There is a negative correlation between protein purity and alkali concentration, and a positive correlation between protein yield and alkali concentration. The highest purity and yield values were obtained at both low temperature and alkali concentration. Therefore, the standard protein extraction conditions still presented the highest purity and yield values. However, such values are still insufficient in terms of optimisation. A new strategy was then proposed to tackle this issue, based on two assumptions: 1) Further extraction of the extracted solid material (starchy residue) with an alkali can increase the yield and potentially the purity of the protein concentrates. 2) Lower alkali concentration can improve both protein yield and purity. The sequential washing experiment results are shown in Table 7. It can be noted that there was an overall increase in both purity and yield with decreasing alkali concentration (NaOH, ChOH and MEA), which confirms hypothesis 2). Additionally, the protein yield increased when compared to the standard condition employed, although the protein purity either remained or slightly decreased for the ChOH and MEA extraction. Therefore, the experiments confirmed both hypotheses and it is concluded that low alkali concentration provide higher yield and purity values. However, a question still remains: if the alkali concentration is decreased, will the yield and purity also increase? To answer this question, a series of diluted alkali extractions were thus performed. Table 7. Protein yield and purity of the sequential washing experiments.

Protein purity and yield values for the dilute alkali sequential washing experiments are shown in Fig.3. In general, there is an opposing trend between protein purity and yield. The highest purity values were achieved at the lowest alkali concentration, 0.01 mol/L for both ChOH and NaOH. Conversely, the highest yield values were achieved at the highest alkali concentration, 0.2 mol/L. In order to achieve both high purity and yield values, the best condition was found to be 0.04 mol/L, with protein purity and yield of 72.9% and 51.1% for NaOH and 75% and 49.7% for ChOH. A mixture of 0.25 mol/L ChOH and 0.25 mol/L MEA provided a protein purity comparable to range of 0.01-0.04 mol/L ChOH, however, the yield was considerably lower, 37%, which rejects the possibility of an enhanced formulation of mixed ChOH and MEA. The best conditions in each type of alkali extraction are shown in Table 8. Based on this, the scaled up experiments were performed. The mass balances for both NaOH and ChOH extraction are shown in Fig.4 and 5. It is possible to achieve 61.4 kg of protein concentrate, namely jackfruit seed protein concentrate (JFSPC), per metric tonne of dry JFS flour. Nearly 630 kg of starch residue is also generated through this process. By using ChOH, nearly 60 kg of JFSPC can also be obtained per metric tonne of JFS and 620 kg of starch residue is produced. Table 8. Best concentration for each alkali type in sequential washing extraction.

Defatting is a common pre-extraction step required prior to protein extraction because it can enhance the protein extraction. However, it often employs the use of volatile organic solvents such as hexane or cyclohexane and, therefore, is not deemed the best option in terms of Green Chemistry principle. Therefore, the alkaline pre-extraction was tested with defatted and unfatted JFS. The values of protein purity and yield are shown in Table 9. It can be seen that there are no significant differences in terms of yield and purity between the two extractions, which proves to be beneficial for the overall process as it short- cuts one pre-extraction step. Table 9. Protein purity and yield for NaOH standard protein extraction (0.1 mol/L, 1 hour, room temperature) without sequential washing.

3. Organoleptic properties Organoleptic properties are the aspects of food, water or other substances that create an individual experience via the senses — including taste, sight, smell, and touch. The organoleptic properties of the protein samples are shown in Table 10. Both JFS protein concentrates presented a brown colour, which is agreement with Ulloa’s et al. (2020) study on alkaline protein extraction of JFS. All the protein samples presented neutral colour, texture, and taste. Table 10. Organoleptic properties of the protein samples.

A large amount of the dried whey protein in the United States is manufactured from Cheddar cheese whey coloured with annatto. Annatto is a natural colouring agent derived from the outer seed coats of the tropical shrub Bixa orellana [39]. The major carotenoids responsible for the yellow colour of annatto are bixin, which is soluble in nonpolar media, and norbixin, which is soluble in polar media. Norbixin is the primary carotenoid derived from annatto used for cheesemilk and the primary colorant in whey. However, coloured whey is generally bleached to achieve a whiter dried product suitable for a wide range of applications. Although carotenoid pigments should not be present in the JFS protein isolates, the brown coloration is likely due to the presence of phenolic compounds from the lignin present in the seeds. Following the same hypothesis, bleaching of JFS protein isolates could potentially make them lighter which would be visually more appealing. Benzoyl Peroxide (BP) and Hydrogen Peroxide (HP) are the two commercially approved bleaching agents used in the United States to bleach liquid whey. The bleaching step applied in the processing of whey protein may affect the flavour of whey protein isolates, as well the functional properties. Listiyani et al. (2011) [40] confirmed that volatile and sensory profiles of unbleached, HP-bleached, and BP-bleached whey protein concentrates were distinct. Jervis et al. (2012) found that both HP and BP are viable bleaching agents for Cheddar cheese whey. Higher off-flavour intensities and lipid oxidation associated with HP bleaching suggest that concentrations and time should be optimised and carefully applied. BP creates less of flavours and bleaches fluid whey more efficiently than HP. BP, however, is not currently an approved bleaching agent for whey products in China or Japan. They also found out that HP may improve the heat stability of rehydrated whey protein concentrate, potentially enhancing its functionality in heat-treated products. 4. Bulk density The bulk density values for some protein samples are shown in Table 11. Table 11. Bulk density values for pea, soy and JFS protein samples.

Bulk density is a measure of the heaviness of a flour sample[41]. The bulk density of flour used to determine its packaging requirements. It is depending on the particle size and moisture content of flours. Bulk density of composite flour increased with an increase in the incorporation of different flours with wheat flour. The high bulk density of flour suggests their suitability for use in food preparations (liquids, semisolids or solids). In contrast, low bulk density would be an advantage in the formulation of weaning foods [41]. The bulk density values obtained for the ChOH and NaOH protein isolates from this study are lower than the commercial soy and pea protein isolates. When compared to other JFS protein isolates, the density values were similar to Ulloa’s et al. (2017), however, Haque’s et al. (2020) presented almost double of the values, which might be related with the drying method employed, spray drying. According to Milán-Carrillo et al. (2000 [42]), the bulk density of legume flour plays an essential role in weaning food formulation, that is, reducing the bulk density of the flour is probably helpful to the formulation of weaning foods. The bulk density reflects the load the sample can carry if allowed to rest directly on one another. 5. Water holding capacity (WHC) The WHC values for the protein isolates studied in this project together with several other types of plant-based protein isolates were shown in Table 12. Table 12. WHC values for plant-based protein concentrates.

WHC plays an important role in developing food texture, especially in comminuted meat products and baked dough. Protein ingredients with very high WHC may dehydrate other ingredients in a food system. Proteins with low WHC can be more sensitive to storage humidity. Therefore, selection of proteins with an appropriate WHC is vital in food formulation [23]. However, various intrinsic, extrinsic, and environmental factors such as pH, ionic strength, and temperature affect the WHC of proteins. For a protein, the lowest WHC is usually recorded at the isoelectric point where the net charge of the protein in a solvent is zero, and protein–protein interactions are dominant. Change in the pH of a protein solution alters the charges on ionizable groups and alters the conformation of proteins by either exposing or concealing water binding sites. WHC values for the ChOH and NaOH protein isolates were lower than the ones obtained for the commercial pea and soy proteins. However, similar values were shown by Haque et al. (2020) [32] and Mahanta and Kalita (2015) [5] with JFS protein isolate and flour respectively, which indicates the data is consistent with the literature. The WHC for both ChOH and NaOH were superior to other types of protein concentrates and isolates such as oats, lentils, chickpea and even pea concentrates (Ma et al., 2022) [41] . Plant proteins with good water and oil holding capacities are often used as meat extenders or in plant-based meat analogs. For instance, the water holding capacity of beef sausage was improved by adding 2.5% bean flour as an extender, which was quantified by measuring the amount of water the sausage could hold when compressed with a 1 kg weight (Ma et al., 2022). It has been reported that the addition of chickpea and pea flour to low-fat pork bologna resulted in a higher cooking yield than the control (less fluid loss), with the chickpea flour giving the best results (>97% yield) (Ma et al., 2022). The purge loss, which is the percentage weight loss of the sample after storage, was also significantly reduced after a plant flour was added to bologna. This study showed that the addition of plant proteins helps maintain the fluids within products during storage, which may improve their quality attributes. Pea protein isolates have been used as meat extenders in chicken nuggets, due to their ability to increase the water holding capacity in a dose-dependent manner (Ma et al., 2022). The overall product cook loss also decreased when pea protein isolate was added, decreasing from 12.4% to 5.0%. This effect is due to more water and oil being retained by the plant proteins in the product. Although the cooking loss was lowered, the overall moisture content of the chicken nuggets decreased when more than 3% pea protein isolate was added, which could impact their desirable sensory attributes. Plant protein concentrates and isolates have also been used as texturized vegetable proteins (TVP) in meat analogs due to their good water holding capacity properties. The WHC influences the porosity and air cell size of the TVPs produced by extrusion (Ma et al., 2022). Traditionally, TVPs were made from soy protein isolates, but other proteins are now being utilized for this purpose, including pea, mung bean, and peanut proteins. 6. Oil Holding Capacity (OHC) The OHC values (g Oil/ g protein) for the protein samples studied in this project together with several other types of plant-based protein isolates were shown in Table 13. Table 13. OHC values for plant-based protein samples.

Binding or entrapping of fat in a food matrix influences the textural and other sensory attributes of the food. Therefore, the ability of proteins to absorb and retain fat and to interact with them in emulsions and other food systems is important in food formulations. Fat absorption by proteins is affected by protein type, processing conditions, protein–amino acid composition, size of the fat particles or oil droplets, and temperature [23]. Protein powders with low-density and small particle size adsorb and entrap more oil than high-density protein powders do [12]. Usually, proteins with lower solubility in water possess higher fat binding capacity [3]. Proteins have little flavour of their own; however, they influence flavour perception by binding flavour-active compounds. The flavour-binding behaviour of proteins is an important consideration in the design of food flavours, especially those intended for low-fat food formulations. Several factors determine the extent of interaction between proteins and food flavours, including the chemical nature of the flavouring compound, temperature, ionic conditions, glassy rubbery nature, physical structure, and processing history of food proteins [3]. OHC values for the ChOH and NaOH protein isolates from this study were superior by more than 2-fold to the values for the pea and soy protein isolates. Additionally, the values were also higher than the ones obtained by Mahanta and Kalita (2015) and Haque et al. (2020) with JFS protein flour and isolate respectively, which places both ChOH and NaOH amongst the protein isolates with the highest OHC values with Oat and Lentil protein concentrates (Table 11). 7. Foaming properties The results for the foaming capacity were shown in Fig.6. The effect of emulsification capacity is clearly poorer at nearly the isoelectric pH of the proteins, 4, at which it demonstrates a low range of capacities, 16-26%. At neutral pH, ChOH and NaOH JFSP concentrates showed similar values to commercial soy and superior values compared to commercial pea concentrates. At high pH, ChOH JFSPC exhibited similar performance to soy and pea and NaOH presented superior performance to pea and soy PCs. In terms of stability, ChOH and NaOH JFSPCs presented performance comparable to soy PC at low pH, exceeded pea and soy at neutral pH, and similar to but inferior to pea and soy respectively at high pH. In general, ChOH and NaOH JFSPCs were superior to pea PC and either superior or similar to pea PC. It was also possible to draw a comparison to Akter’s et al. work on the alkaline extraction of JFS proteins (Fig.7). As it could be seen in Fig.7, foaming capacity and stability values for the ChOH and NaOH JSFPCs were at least 3-fold higher than Akter’s et al. (2020) at neutral pH. At low pH, ChOH and NaOH JFSPCs presented similar foaming capacity values and at least 6-fold higher stability than Akter’s et al. (2020) protein concentrate. It is important to highlight that in this work an optimization of the protein yield and concentration was performed, whereas Akter’s et al. (2020) only used a standard condition from literature. They added 1.0M NaOH to pH 9.0 and then extracted the protein for 1hour at room temperature. However, it is important to also note that, amongst different studies, large variations are reported for mixing speeds and times, which again makes it difficult to make direct comparisons among different studies. For example, blending for a longer time or with a higher speed can result in higher foam volume, affecting the calculation for foaming capacity and stability [41]. 8. Protein solubility Protein solubility as a function of the pH is shown in Fig. 8. ChOH and NaOH JFSPCs presented slightly better results in terms of protein solubility than pea and soy PCs. NaOH JFSPC also showed slightly higher solubility than ChOH JFSPC, especially at pH 3 and 5. In general, the water-solubility of plant proteins is lowest (< 20%) in the pH range from around 4 to 6 because their isoelectric points are within this pH range [41]. As a result, there is a relatively low electrostatic repulsion between the protein molecules, which means they can easily associate with each other through van der Waals, hydrophobic, or hydrogen bonding interactions. Conversely, the solubility of plant proteins usually increases when the pH moves away from their isoelectric point, as this increases their charge and electrostatic repulsion. Therefore, it is recommended that pH levels of 8 or above are used to optimize protein solubility but this is not always practical. Meat products like hamburgers and sausages typically have pH values lower than this, around five to seven depending on the type of meat used, which is close to the isoelectric points of the plant proteins (pH measurement of meat products.). For instance, chorizo sausage containing 3% plant proteins (soy, bean, lentil, or broad bean proteins) as meat extenders had a pH of around 5.8, which is near the isoelectric point of these proteins. In another study, where only plant proteins were used to form a meat analog, the pH was around seven, which meant that the plant proteins were more soluble. It should be noted that it may be beneficial to have both soluble and insoluble proteins in plant-based meat analogs to obtain the desirable textural and other quality attributes. 9. Emulsion properties The emulsion activity and stability values as a function of pH is shown in Fig.9. It can be noted that at low pH, there is no emulsion formation from the soy and pea PCs. This could be due to its proximity to the isoelectric point of pea and soy protein, which makes the proteins less able to act as surfactants due to the lack of a net surface charge. At neutral pH, both ChOH and NaOH JFSPCs outperformed the commercial protein samples by a difference ranging from 12 to 20%. At high pH, NaOH JFSPC presented the best performance and ChOH JFSPC was similar to pea PC. The ability of a protein to stabilize an emulsion is determined by incubating the samples under standardized conditions, such as pH (2–8), ionic strength (0 to 0.5 mol/L NaCl), temperature (30 to 90 ◦C) for a fixed period, and then measuring their particle size distribution, microstructure, and creaming stability. In addition, researchers may carry out zeta-potential, surface hydrophobicity, interfacial tension, and rheology measurements to obtain more insights into the performance of plant protein emulsifiers. It should be noted that the use of different methods and operating conditions to determine the emulsifying properties of plant proteins by different researchers makes it difficult to directly compare their functional performance. Surface active plant proteins can be used to emulsify and bind fat in meat products, such as in frankfurters and patties. For instance, it has been reported that the addition of lupin flour enhanced the emulsion stability of beef sausage [41]. The quantify of fluids and fats released from the sausages decreased as the amount of lupin flour added was increased, thereby leading to a higher cooking yield. Pulse proteins have also been used as emulsifiers to replace egg yolk in salad dressings [41]. The authors showed that lentil, chickpea, and pea protein isolates could be used to produce salad dressings with similar physical properties as commercial egg-based ones. 10. Gelling properties The capacity of gel formation for both ChOH and NaOH JFSPCs were shown in Table 14. In the process of gel formation, about 8% of protein in 1.0 mol/L NaCl solution initiated forming a gel; however, this gel was not consistent enough to withstand the gravity force at the inverted position of the container. At least 12% (w/v) of JFSPC was required to make a firm gel. Akter´s et al. (2020) [32] did not find protein gel formation in pure water. However, their protein load ranged until 14 wt%, whereas in this work, up to 20 wt% was reached. The lower least gelation concentration (LGC) implies the greater gelling capacity of the protein [44]. Table 14. Gelation properties of protein suspensions of ChOH and NaOH JFSPCs.

The LGC is the lowest protein concentration where the protein sample remains in the inverted tube. Although this method provides valuable information about the ability of plant proteins to form gels, it does not provide any information about the properties of the gels formed, such as their hardness or brittleness. Therefore, many researchers use additional methods to measure the textural properties of the gels [41]. The most common means of quantifying the textural properties of gels formed from plant proteins is to use compression tests where stress-strain relationships are recorded as a sample is compressed/decompressed at a fixed rate. For example, texture profile analysis can measure the hardness, adhesiveness, springiness, cohesiveness, gumminess, and resilience of gels. Using this method, it has been reported that gels formed from lupine proteins had a higher hardness than those formed from pea or fava bean proteins. Dynamic shear rheology measurements can also characterize gel properties, particularly as a function of temperature. For example, Langton and co-workers[45] studied the gelation process of fava bean protein mixtures at pH 5 and 7 as a function of temperature (25 to 95 °C) using dynamic oscillatory measurements. They reported an increase in storage modulus (G’) at a lower temperature, for pH 5 gels compared with pH 7 gels. Other researchers showed that gels formed from kidney bean protein had higher strength and thermal stability than those formed from pea protein. These methods can also determine the gelation temperature and whether a gel is thermally reversible or irreversible. The gelation properties of plant proteins depend on their nature. The LGC of most plant proteins falls within the range of 10–18%, but some of them can form gels at considerably lower concentrations. For instance, chickpea proteins have a LGC value of around 5–7%. It should be noted that the reported LGC values depend on gelation conditions, such as pH, ionic strength, and heating conditions, as well as on protein type and the presence of other ingredients. Consequently, the same protein may have different LGC values depending on the conditions used, highlighting the importance of standardizing conditions when comparing different protein sources. Plant proteins are often used as gelling agents to improve the textural attributes of meat products. For instance, it has been reported that the addition of chickpea and lentil flour into beef burgers resulted in a higher hardness. Similarly, adding a chickpea protein concentrate to sausages increased their gel strength. In a different study, it was reported that adding 20% or 60% chicken meat to soy-based sausage did not alter their gel strength or other textural attributes, such as cohesiveness, chewiness, stiffness, adhesiveness, and gumminess [64]. However, the chicken meat-free version of the sausage had a lower gel strength than the hybrid sausages, which may have been due to the higher amount of water in this formulation. Therefore, there is great potential in applying plant proteins in making hybrid meat products to reduce meat consumption and meat-free products. Researchers have compared the impact of using soy, pea, lentil, and bean proteins as meat extenders in beef patties on their textural properties [65]. They found that the beef patties containing soy protein had the highest hardness, gumminess, and chewiness. The reason why beef patties containing pulse proteins had lower textural attributes may have been because they had a lower protein content (55–60%) than the soy protein ingredient used (90%). Fabia bean flour has been used to create plant protein-based emulsion gels, including yogurt and tofu analogs [66]. Removal of starch from the fava bean flour resulted in a tofu analog with a stronger texture and higher water holding capacity, which mainly can be attributed to the increased protein content. 11. Amino acid profile Amino acid profile values for the raw JFS and both ChOH and NaOH protein concentrates obtained are shown in Table 15. The optimization of protein extraction was able to increase the amino acid concentration in the protein concentrates, especially with aspartic acid, glutamic acid (Glu/E), glycine (Gly/G) and leucine (Leu/L). The essential amino acid content of ChOH and NaOH were 27 and 28.6% respectively. Essential amino acid contents usually are lower in plant-based (26 ± 2% of total protein) when compared with animal-based proteins (37 ± 2% of total protein) and human skeletal muscle protein (38% of total protein) [46]. The essential amino acid contents of the plant-based proteins oat (21%), lupin (21%), wheat (22%), hemp (23%), and microalgae (23%) are below the World Health Organisation/Food and Agriculture Organisation/UNU amino acid requirements. However, the essential amino acid requirement would be met when either ChOH or NaOH JFSPCs are the sole protein sources consumed. Note that the requirement is based on a recommended adult protein intake of 0.66 g/kg body weight per day. Plant-based proteins that do meet the requirements for essential amino acids include soy (27%), brown rice (28%), pea (30%), corn (32%), and potato (37%). Of the animal-based proteins, whey protein had the highest essential amino acid content of 43%. Table 15. Amino acid profile of raw JFS, ChOH and NaOH JFSPCs.

Gorrisen et al. (2018) [47] also showed that the average phenylalanine and methionine content in plant-based protein isolates is 3.8% and 1.5% (Fig. 10a and b). ChOH and NaOH JFSPCs presented exceptionally higher phenylalanine, 8.1 and 7.9%, and methionine content, 6.5% and 6.8%, both of which are essential amino acids, making JFSPCs an interesting choice as a source for these amino acids. Conclusions The protein content of the raw JFS flours were of little significance across the samples. The optimised ChOH and NaOH alkaline extraction process was able to increase the overall yield and purity of the protein concentrates. The essential amino acid content of the JFSPCs ranged from 27-28%, which is sufficient for use as the only protein source. Compared to pea and soy PCs, the JFSPCs presented lower bulk density and WHC values. 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Claims

Claims: 1. A process for extracting a protein concentrate from jackfruit seed comprising: processing jackfruit seed to provide a jackfruit seed composition with reduced particle size; treating the jackfruit seed composition with reduced particle size with a solution comprising an amine to provide a mixture with a solid phase and a liquid phase comprising jackfruit seed protein; and recovering the jackfruit seed protein concentrate from the liquid phase.

2. The process of claim 1, wherein the amine is selected from the group consisting of monoethanolamine and choline hydroxide.

3. The process of claim 2, wherein the amine is choline hydroxide.

4. The process of any one of claims 1 to 3, wherein the pH of the solution comprising an amine is from pH 7.0 to 12.0.

5. The process of any one of claims 1 to 4, wherein the pH of the solution comprising an amine is from pH 8.0 to 10.0.

6. The process of any one of claims 1 to 5, further comprising defatting the jackfruit seed composition with reduced particle size prior to treating the jackfruit seed composition with reduced particle size with a solution comprising an amine.

7. The process of any one of claims 1 to 6, wherein the step of recovering the jackfruit seed protein concentrate from the liquid phase comprises isoelectric precipitation.

8. The process of any one of claims 1 to 7, further comprising drying the recovered jackfruit seed protein concentrate.

9. The process of any one of claims 1 to 8, further comprising formulating the recovered jackfruit seed protein concentrate with one or more additional proteins, lipids or carbohydrates.

10. The process of claim 9, wherein the one or more additional proteins, lipids or carbohydrates are separate preparation from jackfruit.

11. The process of any one of claims 9 to 10, wherein the one or more additional proteins, lipids or carbohydrates are from a source other than jackfruit.

12. The process of any one of claims 9 to 11, further comprising producing a food product from the formulation.

13. The process of claim 12, wherein the food product is a meat substitute.

14. The process of any one of claims 1 to 13, wherein the step of treating the jackfruit seed composition with reduced particle size with a solution comprising an amine to provide a mixture with a solid phase and a liquid phase comprising jackfruit seed protein comprises adding the amine to a concentration of from 0.02 to 0.06 mol/L in the liquid phase.

15. A process for extracting a protein concentrate from jackfruit seed comprising: processing jackfruit seed to provide a jackfruit seed composition with reduced particle size; treating the jackfruit seed composition with reduced particle size with a solution comprising an alkali to provide a mixture with a solid phase and a liquid phase comprising jackfruit seed protein, wherein the alkali is added to a concentration of from 0.02 to 0.06 mol/L; and recovering the jackfruit seed protein concentrate from the liquid phase.

16. The process of claim 15, wherein the alkali is added to a concentration of from 0.03 to 0.05 mol/L.

17. The process of claim 15, wherein the alkali is added to a concentration of from 0.035 to 0.045 mol/L.

18. The process of any one of claims 15 to 17, wherein the alkali is selected from the group consisting of sodium hydroxide, monoethanolamine, and choline hydroxide.

19. The process of claim 18 wherein the amine is choline hydroxide

20. The process of any one of claims 15 to 19, wherein the pH of the solution comprising an amine is from pH 7.0 to 12.0.

21. The process of any one of claims 15 to 20, wherein the pH of the solution comprising an amine is from pH 8.0 to 10.0.

22. The process of any one of claims 15 to 21, further comprising defatting the jackfruit seed composition with reduced particle size prior to treating the jackfruit seed composition with reduced particle size with a solution comprising an amine.

23. The process of any one of claims 15 to 22, wherein the step of recovering the jackfruit seed protein concentrate from the liquid phase comprises isoelectric precipitation.

24. The process of any one of claims 15 to 23, further comprising drying the recovered jackfruit seed protein concentrate.

25. The process of any one of claims 15 to 24, further comprising formulating the recovered jackfruit seed protein concentrate with one or more additional proteins, lipids or carbohydrates.

26. The process of claim 25, wherein the one or more additional proteins, lipids or carbohydrates are separate preparation from jackfruit.

27. The process of any one of claims 25 to 26, wherein the one or more additional proteins, lipids or carbohydrates are from a source other than jackfruit.

28. The process of any one of claims 25 to 27, further comprising producing a food product from the formulation.

29. The process of claim 28, wherein the food product is a meat substitute.

30. The process of any one of claims 1 to 29, wherein the jackfruit seed protein concentrate is characterized by having one or more of the following properties: a) a foaming capacity of from 50% to 80% at pH 7.0; b) a foaming stability of greater than 70% at pH 7.0; c) an emulsion activity of from 60% to 80% at pH 7.0; d) an emulsion stability of greater than 70% at pH 7.0; e) an oil holding capacity of from 1.8 to 2.5 gram oil/gram protein; f) an essential amino acid content of from 22 to 34%; g) a phenylalanine content of from 4.5% to 5.5%; and h) a methionine content of from 3.6% to 4.6%.

31. The process of claim 30, wherein the jackfruit seed protein concentrate is characterized by having two or more of properties a) to h).

32. The process of claim 30, wherein the jackfruit seed protein concentrate is characterized by having three or more of properties a) to h).

33. The process of claim 30, wherein the jackfruit seed protein concentrate is characterized by having four or more of properties a) to h).

34. The process of claim 30, wherein the jackfruit seed protein concentrate is characterized by having five or more of properties a) to h).

35. The process of claim 30, wherein the jackfruit seed protein concentrate is characterized by having six or more of properties a) to h).

36. The process of claim 30, wherein the jackfruit seed protein concentrate is characterized by having seven or more of properties a) to h).

37. The process of claim 30, wherein the jackfruit seed protein concentrate is characterized by having all eight of properties a) to h).

38. The process of any one of claims 1 to 37, wherein the jackfruit seed protein concentrate is further characterized as having a protein content of from 70% to 80% on a dry weight basis.

39. The process of any one of claims 1 to 38, wherein the process provides a protein yield of from 45% to 55%.

40. A jackfruit seed protein concentrate produced according to the process of any one of claims 1 to 8, 15 to 24, or 30-39.

41. A jackfruit seed protein concentrate formulation produced according to the process of any one of claims 9 to 11 or 25 to 27 or 30-39.

42. A food product produced according to the process of any one of claims 12 to 13, 28 to 29, or 30-39.

43. A jackfruit seed protein concentrate characterized by having one or more of the following properties: a) a foaming capacity of from 50% to 80% at pH 7.0; b) a foaming stability of greater than 70% at pH 7.0; c) an emulsion activity of from 60% to 80% at pH 7.0; d) an emulsion stability of greater than 70% at pH 7.0; e) an oil holding capacity of from 1.8 to 2.5 gram oil/gram protein; f) an essential amino acid content of from 22 to 34%; g) a phenylalanine content of from 4.5% to 5.5%; and h) a methionine content of from 3.6% to 4.6%.

44. The jackfruit seed protein concentrate of claim 43, wherein the jackfruit seed protein concentrate is characterized by having two or more of properties a) to h).

45. The jackfruit seed protein concentrate of claim 43, wherein the jackfruit seed protein concentrate is characterized by having three or more of properties a) to h).

46. The jackfruit seed protein concentrate of claim 43, wherein the jackfruit seed protein concentrate is characterized by having four or more of properties a) to h).

47. The jackfruit seed protein concentrate of claim 43, wherein the jackfruit seed protein concentrate is characterized by having five or more of properties a) to h)

48. The jackfruit seed protein concentrate of claim 43, wherein the jackfruit seed protein concentrate is characterized by having six or more of properties a) to h).

49. The jackfruit seed protein concentrate of claim 43, wherein the jackfruit seed protein concentrate is characterized by having seven or more of properties a) to h).

50. The jackfruit seed protein concentrate of claim 43, wherein the jackfruit seed protein concentrate is characterized by having all eight of properties a) to h).

51. The jackfruit seed protein concentrate of any one of claims 43 to 50, wherein the jackfruit seed protein concentrate is further characterized as having a protein content of from 70% to 80% on a dry weight basis.

52. A multicomponent food composition comprising the jackfruit seed protein concentrate produced according to any one of claims any one of claims 1 to 8, 15 to 24, or 30-39 or the jackfruit seed protein concentrate of any one of claims 43 to 51.

53. The multicomponent food composition of claim 52, wherein the composition is characterized in comprising from 0.1% to 50% (w/w), 0.1% to 20% (w/w), 0.1% to 10% (w/w), or 0.1% to 5% (w/w) of the jackfruit seed protein concentrate.

54. The multicomponent food composition of any one of claims 52 to 53, further comprising an additional plant protein.

55. The multicomponent food composition of claim 54, wherein the additional plant protein is from a source other than jackfruit.

56. The multicomponent food composition of claim 55, wherein the additional plant protein is selected from the group consisting of proteins from grains, oil seeds, leafy greens, biomass crops, root vegetables, and legumes.

57. The multicomponent food composition of claim 56, wherein the grains are selected from the group consisting of corn maize rice wheat barley rye triticale and teff

58. The multicomponent food composition of claim 56, wherein the oilseeds are selected from the group consisting of cottonseed, sunflower seed, safflower seed, and rapeseed.

59. The multicomponent food composition of claim 56, wherein the leafy greens are selected from the group consisting of lettuce, spinach, kale, collard greens, turnip greens, chard, mustard greens, dandelion greens, broccoli, and cabbage.

60. The multicomponent food composition of claim56, wherein the biomass crops are selected from the group consisting of switchgrass, miscanthus, sorghum, alfalfa, corn stover, green matter, sugar cane leaves and leaves of trees.

61. The multicomponent food composition of claim 56, wherein the root crops are selected from the group consisting of cassava, sweet potato, potato, carrots, beets, and turnips.

62. The multicomponent food composition of claim 56, wherein the legumes are selected from the group consisting of clover, cowpeas, English peas, yellow peas, green peas, soybeans, fava beans, lima beans, kidney beans, garbanzo beans, mung beans, pinto beans, lentils, lupins, mesquite, carob, soy, and peanuts, vetch (vicia), stylo (stylosanthes), arachis, indigofera, acacia, leucaena, cyamopsis, and sesbania.

63. The multicomponent food composition of any one of claims 52 to 62, further comprising a fat.

64. The multicomponent food composition of claim 63, wherein the fat is selected from the group consisting of corn oil, olive oil, soy oil, peanut oil, walnut oil, almond oil, sesame oil, cottonseed oil, rapeseed oil, canola oil, safflower oil, sunflower oil, flax seed oil, algal oil, palm oil, palm kernel oil, coconut oil, babassu oil, shea butter, mango butter, cocoa butter, wheat germ oil, rice bran oil, an oil produced by bacteria, an oil produced by archaea, an oil produced by fungi, an oil produced by genetically engineered bacteria, an oil produced by genetically engineered algae, an oil produced by genetically engineered archaea, and an oil produced by genetically engineered fungi, and a mixture of two or more thereof.

65. The multicomponent food composition of any one of claims 52 to 64, further characterized in comprising between 10-30% w/w protein, between 5-80% w/w water, and between 5-70% fat.