WO2021217265A1

WO2021217265A1 - Method of producing protein products with reduced off-flavours

Info

Publication number: WO2021217265A1
Application number: PCT/CA2021/050595
Authority: WO
Inventors: Michael Todd NICKERSON; Burcu GÜLDIKEN; Richard Christopher Green; Anusha Geethangani Perera SAMARANAYAKA
Original assignee: University Of Saskatchewan; POS Management Corp.
Priority date: 2020-04-29
Filing date: 2021-04-29
Publication date: 2021-11-04

Abstract

The present application relates to a method of producing protein products comprising extracting water soluble protein extracts from pulse or hemp, and de-flavouring the water soluble protein extract using suitable non-polar resins. Further, the present application relates to the protein products produced using the methods of the present application and uses thereof. The present application also relates to food and/or health products formulated with the protein products.

Description

TITLE: METHOD OF PRODUCING PROTEIN PRODUCTS WITH REDUCED OFF-

FLAVOURS

CROSS-REFERENCE TO RELATED APPLICATIONS

[0001] The present application claims the benefit of priority from U.S. patent application no. 63/017,123, filed on April 29, 2020, the contents of which are incorporated herein by reference in their entirety.

FIELD

[0002] The present application relates to methods of producing protein products, in particular protein products that have reduced off-flavours. Further, the present application relates to the protein products produced using the methods of the present application and uses thereof. In particular, the application relates to methods of producing pulse protein products and hemp protein products that have reduced off-flavours, and the products produced therefrom.

INTRODUCTION

[0003] The global protein ingredient market was valued at $31.8 billion in 2016 and is expected to rise to $46.4 billion by 2022, with the greatest growth occurring in the plant protein ingredient sector. In 2054, it is estimated that 1/3 of all global protein consumed will be of plant origin. Overarching drivers leading to the market shift towards increased plant protein consumption include: a) population growth, with the world population expected to reach 9-10 billion people by 2050; b) increased need for sustainable agronomic practices with reduced water usage; c) urbanization, as populations migrate towards urban centers from rural areas; d) changing demographics, to consumers demanding innovative products which are highly nutritious, good tasting proteins; and e) emerging regulatory influencers, with countries, including China, the Netherlands, France and Denmark, moving to change dietary guidelines to restrict meat consumption in favour of other protein alternatives.

[0004] North America represents the largest market for protein ingredient utilization and growth, followed by Europe and Asia Pacific. In these regions, market trends are also shifting towards lower cost more abundant plant-based alternatives (although markets are still dominated animal-based proteins) due to rising costs of dairy-based ingredients, and growing dietary preferences based on religious, moral or ethical beliefs. Other market drivers include the rising demand in the functional food, beverage and breakfast food sectors as consumers move their purchasing power towards healthier ingredients/products. The leading emerging non-soy protein alternative comes from pea, however other pulses (e.g., lentils, fava beans, chickpeas, lupin and edible beans), oilseeds (e.g., canola, flax and hemp), and cereals (e.g., wheat, barley and oats) are also of substantial interest. In terms of product development, the majority of plant protein research to date has focused on meat alternatives or meat/plant hybrids, sports nutrition bars, high protein non-dairy beverages and breakfast cereals/snacks. However, protein innovations are also occurring across all market segments. Plant proteins have a significant price advantage over animal-based ingredients; for instance, casein is sold for ~$4.90 (USD) a pound, compared to soy or other plant proteins, which range between $0.42 to $2.08 (USD) per pound.

[0005] Currently, techniques for producing pulse protein product exist. For example, W02016015151A1 describes a process of producing a pulse protein product having a protein content of at least about 60wt% using dialysis or membrane filtration. WO2018157262A1 describes a method to produce a pulse protein material soluble at pH 2 to 7 comprising hydrolyzing the pulse protein. W02014008578A1 describes an aqueous solution containing pulse protein product having a protein content of at least 60wt% where the pulse protein is soluble at pH of less than 4.4. US20140093626A1 describes a pulse protein product having a protein content of at least 60wt% prepared by extraction of pulse material with aqueous calcium salt solution and membrane filtration. WO2011137524A1 describes a method of producing a pulse protein product by extracting with calcium salt solution.

[0006] Despite experiencing market growth, the wide spread use of plant proteins has been hindered by their reduced solubility (and functionality) relative to animal-based products, in some cases allergenicity (e.g., fava bean and canola), strong flavour compounds that can negatively affect consumer perception, and tendency to cause flatulence due to carbohydrates and/or oligosaccharides that may be present in the protein product. Therefore, there exists a need to develop a process to produce pulse protein products that are soluble and free of strong flavour compounds.

SUMMARY

[0007] In one aspect, the present application includes a method of producing a pulse protein product comprising: a) extracting a pulse protein source with an aqueous solution having a pH greater than about 8.5 to obtain an alkaline water soluble pulse protein extract and residual pulse protein source; b) separating the alkaline water soluble pulse protein extract from the residual pulse protein source; c) passing the alkaline water soluble pulse protein extract through a non-polar adsorption resin that removes flavouring compounds to obtain a de-flavoured alkaline water soluble pulse protein extract; d) adjusting the pH of the de-flavoured alkaline water soluble pulse protein extract to reach its isoelectric point to precipitate the pulse protein product; e) optionally collecting the pulse protein product from d); f) optionally pasteurizing the pulse protein product from e); g) optionally flash cooling the pasteurized pulse protein product from f); and h) optionally spray drying the flash cooled pulse protein product from g). [0008] In another aspect, the present application includes a pulse protein product produced by a method of the present application.

[0009] In another aspect, the present application includes a use of the pulse protein product of the present application to prepare a food and/or health product.

[0010] In another aspect, the present application includes a food and/or health product comprising the pulse protein product of the present application.

[0011] The present application also includes a method of producing a hemp protein product comprising: a) extracting a hemp protein source with an aqueous solution having a pH greater than about 8.5 to obtain an alkaline water soluble pulse protein extract and residual hemp protein source; b) separating the alkaline water soluble hemp protein extract from the residual hemp protein source; c) passing the alkaline water soluble hemp protein extract through a non-polar adsorption resin that removes flavouring compounds to obtain a de-flavoured alkaline water soluble hemp protein extract; d) adjusting the pH of the de-flavoured alkaline water soluble hemp protein extract to reach its isoelectric point to precipitate the hemp protein product; e) optionally collecting the hemp protein product from d); f) optionally pasteurizing the hemp protein product from e); g) optionally flash cooling the pasteurized hemp protein product from f); and h) optionally spray drying the flash cooled pulse protein product from g).

[0012] In an embodiment, the hemp protein source is de-fatted prior to extraction step a). In an embodiment, the hemp protein source is a milled press cake, for example from whole or dehulled hemp seeds.

[0013] Other features and advantages of the present application will become apparent from the following detailed description. It should be understood, however, that the detailed description and the specific examples, while indicating embodiments of the application, are given by way of illustration only and the scope of the claims should not be limited by these embodiments, but should be given the broadest interpretation consistent with the description as a whole.

DESCRIPTION OF VARIOUS EMBODIMENTS I. Definitions

[0014] Unless otherwise indicated, the definitions and embodiments described in this and other sections are intended to be applicable to all embodiments and aspects of the present application herein described for which they are suitable as would be understood by a person skilled in the art.

[0015] The term “and/or” as used herein means that the listed items are present, or used, individually or in combination. In effect, this term means that “at least one of” or “one or more” of the listed items is used or present.

[0016] As used in the present application, the singular forms “a”, “an” and “the” include plural references unless the content clearly dictates otherwise. For example, an embodiment including “a protein source” should be understood to present certain aspects with one protein sounds or two or more additional protein sources.

[0017] In embodiments comprising an “additional” or “second” component, such as an additional or second protein source, the second component as used herein is different from the other components or first component. A “third” component is different from the other, first, and second components, and further enumerated or “additional” components are similarly different.

[0018] In understanding the scope of the present application, the term “comprising” and its derivatives, as used herein, are intended to be open ended terms that specify the presence of the stated features, elements, components, groups, integers, and/or steps, but do not exclude the presence of other unstated features, elements, components, groups, integers and/or steps. The foregoing also applies to words having similar meanings such as the terms, “including”, “having” and their derivatives. The term “consisting” and its derivatives, as used herein, are intended to be closed terms that specify the presence of the stated features, elements, components, groups, integers, and/or steps, but exclude the presence of other unstated features, elements, components, groups, integers and/or steps. The term “consisting essentially of”, as used herein, is intended to specify the presence of the stated features, elements, components, groups, integers, and/or steps as well as those that do not materially affect the basic and novel characteristic(s) of features, elements, components, groups, integers, and/or steps.

[0019] The terms "about", “substantially” and “approximately” as used herein mean a reasonable amount of deviation of the modified term such that the end result is not significantly changed. These terms of degree should be construed as including a deviation of at least ±5% of the modified term if this deviation would not negate the meaning of the word it modifies or unless the context suggests otherwise to a person skilled in the art.

[0020] The present description refers to a number of chemical terms and abbreviations used by those skilled in the art.

[0021] The term “pulse” as used herein refers the dried edible seeds of certain plants of the legume family.

[0022] The term “hemp” includes all species of the Cannabis plant genus. [0023] The terms “de-fat”, or the like, and “de-fatted”, or the like, as used herein refers to a process of removing fat or oil from a material and material with fat removed, respectively, such as the protein products disclosed herein. When the fat being removed is a liquid at room temperature, the fat is referred to as an oil and the terms “de-oil” and “de-oiled” may be substituted interchangeably for “de-fat” and “de-fatted”, respectively.

[0024] The terms “removing” and “removed” with respect to the fat or oil in a material, means that the amount of endogenous fat/oil in the material has been reduced to amount where it is negligible or where it does not have any negative effects on subsequent processing steps. Therefore, “de-fatted” or “de-oiled” materials may contain 0% to about 30% of its endogenous fat/oil.

[0025] The term “press cake” as used herein refers to the protein and fiber rich material obtained after expeller pressing of whole, flaked, or dehulled seeds by pre heating followed by pressing to remove the majority of the endogenous oil of the seeds.

[0026] The term “alkaline” as used herein refers to a pH that is greater than 7.

[0027] The term “isoelectric pH” or “isoelectric point” as used herein for protein precipitation methods, is the pH at which the protein molecules have a net zero charge, and therefore, precipitate out of an aqueous-based solution.

[0028] The term “water hydration capacity” or “water holding capacity” of a protein product as used herein is a measurement of a protein’s ability to prevent water from being released or expelled from their three-dimensional structure.

[0029] The “oil holding capacity” of a protein as used herein is a measurement of a protein’s ability to prevent oil from being released or expelled from their three- dimensional structure.

[0030] The terms foam capacity (FC) and foam stability (FS) as used herein are measurements of a protein’s ability to form and maintain foam.

II. Methods of the Present Application

[0031] In one aspect, the present application includes a method of producing a pulse protein product comprising a) extracting a pulse protein source with an aqueous solution having a pH greater than about 8.5 to obtain an alkaline water soluble pulse protein extract and residual pulse protein source; b) separating the alkaline water soluble pulse protein extract from the residual pulse protein source; c) passing the alkaline water soluble pulse protein extract through a non-polar adsorption resin that removes flavouring compounds to obtain a de-flavoured alkaline water soluble pulse protein extract; d) adjusting the pH of the de-flavoured alkaline water soluble pulse protein extract to reach its isoelectric point to precipitate the pulse protein product; e) optionally collecting the pulse protein product from d); f) optionally pasteurizing the pulse protein product from e); g) optionally flash cooling the pasteurized pulse protein product from f); and h) optionally spray drying the flash cooled pulse protein product from g).

[0032] In some embodiments, the pulse protein source is any suitable edible pulse protein source. In some embodiments, the pulse protein source is selected from chickpeas, lentils, beans and peas and combinations thereof. In some embodiments, the lentils are red, green, brown, and/or black lentils. In some embodiments, the lentils are red and/or green lentils. In some embodiments, the beans are fava beans which are beans of the species Vida faba. In some embodiments, the peas are green and/or yellow peas.

[0033] In some embodiments, the pulse protein source is ground and/or milled pulse. In some embodiments, the pulse protein source is milled by dry milling and/or wet milling. In some embodiments, the pulse protein source is pulse flour.

[0034] In some embodiments, the ratio of the pulse protein source to the aqueous solution is about 1 :5 to about 1 :20. For example, the ratio is about 1 :10.

[0035] In some embodiments, the extracting of the pulse protein is at a temperature of about 10°C to about 55°C. In some embodiments, the extracting of the pulse protein is at a temperature of about 15°C to about 45°C. In some embodiments, the temperature is about 18°C. [0036] In some embodiments, the pH of the aqueous solution is about 8.5 to about 12, about 8.5 to about 11.5, or about 9.0 to about 11.0. In some embodiments, the pH is about 9.5.

[0037] In some embodiments, the alkaline water soluble pulse protein extract is separated from the residual protein source using any suitable physical separation means, such as filtration and/or centrifuge. In some embodiments, the alkaline water soluble pulse protein extract is separated from the residual protein source using a decanter centrifuge.

[0038] In some embodiments, the non-polar adsorption resin comprises porous particles having an average pore diameter of about 0.2 mm to about 1.5 mm. In some embodiments, the average pore diameter is about 0.5 mm. In some embodiments, the non-polar adsorption resin comprises spherical or macroreticular porous particles.

[0039] In some embodiments, the non-polar adsorption resin is any non-polar synthetic polymer resin suitable for adsorption of flavour components. In some embodiments, the non-polar adsorption resin comprises a polyaromatic polymer polyaromatic co-polymer, a polymethylacrylate polymer or a polymethylacrylate co polymer. In some embodiments, the polyaromatic polymer or polyaromatic co-polymer is, polystyrene, polydivinylbenzene, or polystyrene-divinylbenzene co-polymer. In some embodiments, suitable non-polar adsorption resins include Diaion™ HP20, Amberlite™ XAD-16, Amberlite™ FPX66, and other suitable resins.

[0040] In some embodiments, the alkaline water soluble pulse protein extract is passed through the non-polar adsorption resin with a flow rate of about 200 kg/h to about 700 kg/h. In some embodiments, the flow rate is about 500 kg/h.

[0041] In some embodiments, the ratio of resin volume to alkaline water soluble pulse protein extract volume is about 1 : 100 to about 1 :200, or about 1 : 120 to about 1 : 130.

[0042] In some embodiments, the isoelectric point of the de-flavoured alkaline water soluble pulse protein extract will vary depending on the identity of the protein as is known to those skilled in the art. In some embodiments, the isoelectric point of the de- flavoured alkaline water soluble pulse protein extract is about pH 4 to about pH 6, or about pH 4.5. [0043] In some embodiments, the pH of the de-flavoured alkaline water soluble pulse protein extract is adjusted with an organic acid. In some embodiments, the acid is any suitable food grade acid, such as citric acid, hydrochloric acid or phosphoric acid, or a mixture thereof.

[0044] In some embodiments, step d) of the method of the present application further comprises holding the pH of the de-flavoured alkaline water soluble pulse protein extract at its isoelectric point for about 15 minutes to about 45 minutes, or for example for about 30 minutes.

[0045] In some embodiments, the pulse protein product of step d) is collected using a centrifuge. For example, the centrifuge is a desludger centrifuge.

[0046] In some embodiments, the pulse protein product from step e) is pasteurized using a jet cooker.

[0047] In some embodiments, the pulse protein product from step e) is pasteurized at about 100°C to about 150°C for about 5 seconds to about 25 seconds, for example, at 120°C for about 15 seconds.

[0048] In some embodiments, the pulse protein product from step e) is optionally neutralized prior to being pasteurized.

[0049] In some embodiments, the pulse protein product from step e) is optionally adjusted to about 5% solids to about 20% solids prior to being pasteurized. In some embodiments, the pulse protein product is adjusted to about 10% solids prior to being pasteurized.

[0050] In some embodiments, the pulse protein product from step f) is flash cooled to about 50°C to about 60°C. In some embodiments, the flash cooling is performed under vacuum. In some embodiments, performing the flash cooling removes greater amounts of volatile flavour components.

[0051] In some embodiments, the pulse protein product from step g) is spray dried, optionally using a benchtop spray drier.

[0052] The present application also includes a method of producing a hemp protein product comprising: a) extracting a hemp protein source with an aqueous solution having a pH greater than about 8.5 to obtain an alkaline water soluble pulse protein extract and residual hemp protein source; b) separating the alkaline water soluble hemp protein extract from the residual hemp protein source; c) passing the alkaline water soluble hemp protein extract through a non-polar adsorption resin that removes flavouring compounds to obtain a de-flavoured alkaline water soluble hemp protein extract; d) adjusting the pH of the de-flavoured alkaline water soluble hemp protein extract to reach its isoelectric point to precipitate the hemp protein product; e) optionally collecting the hemp protein product from d); f) optionally pasteurizing the hemp protein product from e); g) optionally flash cooling the pasteurized hemp protein product from f); and h) optionally spray drying the flash cooled pulse protein product from g).

[0053] In some embodiments, the hemp is any species of the Cannabis plant genus, including, but not limited to Cannabis sativa, Cannabis indica , and Cannabis ruderalis.

[0054] In some embodiments, the hemp protein source is hemp seed, stalk and/or leaves. In some embodiments, the hemp protein source is hemp seed, flaked hemp seed, and/or hemp seed press cake. In some embodiments the hemp protein source is defatted hemp seed. In some embodiments, the hemp protein source is defatted hemp seed press cake, optionally a milled hemp seed press cake from whole or dehulled hemp seed. In some embodiments, the press cake has about 70% to about 100% of the endogenous oil of the seeds removed. In some embodiments, the press case has about 70% to about 85% of the endogenous oil in the seeds removed.

[0055] In some embodiments the hemp seed is defatted using any known method, for example, but limited to expeller pressing (i.e. screw pressing), cold pressing or by producing expanded pellets (produced using expander pelletizers) followed by extraction of the oil using an organic solvent such as n-hexane and/or isohexane. [0056] In some embodiments, expeller pressing is done by pre-heating hemp seeds or flaked hemp seeds to inactivate lipid oxidizing enzymes, flaking to facilitate pressing, then pressing to remove approximately 70 - 85% of the oil in the seeds. In some embodiments, the resulting hemp seed press cake contains about 12% oil.

[0057] In some embodiments, cold pressing is done by pressing hemp seeds using conditions to maintain a press cake and oil temperature below 70 °C. Typically, the pressing equipment has a cooling jacket to control pressing temperature and two pressings may be applied (double pressing). In some embodiments, the resulting hemp seed press cake still contains 7% to 12% oil and will be used for protein extraction.

[0058] In some embodiment, solvent extraction is done by extracting expanded pellets of hemp seed meal (produced using expander pelletizers) using an organic solvent such as n-hexane and/or isohexane. The resulting solvent extracted hemp seed meal is de-solventized under heat and potentially by also drawing some vacuum. In some embodiments, the de-solventizing temperature of the meal reaches over about 100 °C in a desolventizer-toaster. However, in some embodiments, if vacuum is applied the temperature may be kept below about 65 °C. In some embodiments, solvent extracted meal will contain less than 1% oil.

[0059] In some embodiments, if non-defatted hemp protein source is used the method of the application further includes a step of fat removal during the protein extraction (step a), for example using a cream separator or a disc-stack centrifuge set up as a three-phase (solid/liquid/liquid) or two-phase (liquid/liquid) separator.

[0060] In some embodiments, the ratio of the hemp protein source to the aqueous solution is about 1 :4 to about 1 :20. For example, the ratio is about 1 :10. For example, the ratio is about 1 :5.

[0061] In some embodiments, the extracting of the hemp protein is at a temperature about 10°C to about 55°C. In some embodiments, the extracting of the hemp protein is at a temperature about 15°C to about 55°C. In some embodiments, the temperature is about 50°C.

[0062] In some embodiments, the pH of the aqueous solution is about 8.5 to about 12, about 8.5 to about 11.5, or about 9.0 to about 11.5. In some embodiments, the pH is about 11.0. [0063] In some embodiments, the alkaline water soluble hemp protein extract is separated from the residual protein source using any suitable physical separation means, such as filtration and/o centrifuge. In some embodiments, the alkaline water soluble hemp protein extract is separated from the residual protein source using a decanter centrifuge.

[0064] In some embodiments, the non-polar adsorption resin comprises porous particles having an average pore diameter of about 0.2 mm to about 1.5 mm. In some embodiments, the average pore diameter is about 0.5 mm. In some embodiments, the non-polar adsorption resin comprises spherical or macroreticular porous particles.

[0065] In some embodiments, the non-polar adsorption resin is any non-polar synthetic polymer resin suitable for adsorption of flavour components. In some embodiments, the non-polar adsorption resin comprises a polyaromatic polymer, a polyaromatic co-polymer, a polymethylacrylate polymer or a polymethylacrylate co polymer. In some embodiments, the polyaromatic polymer or polyaromatic co-polymer is, polystyrene, polydivinylbenzene, or polystyrene-divinylbenzene co-polymer. In some embodiments, suitable non-polar adsorption resins include Diaion™ HP20, Amberlite™ XAD-16, Amberlite™ FPX66, and other suitable resins.

[0066] In some embodiments, the alkaline water soluble hemp protein extract is passed through the non-polar adsorption resin with a flow rate of about 200 kg/h to about 700 kg/h. In some embodiments, the flow rate is about 500 kg/h.

[0067] In some embodiments, the ratio of resin volume to alkaline water soluble pulse protein extract volume is about 1 : 100 to about 1 :200, or about 1 : 120 to about 1 : 130.

[0068] In some embodiments, the isoelectric point of the de-flavoured alkaline water soluble hemp protein extract will vary depending on the identity of the protein as is known to those skilled in the art. In some embodiments, the isoelectric point of the de- flavoured alkaline water soluble hemp protein extract is about pH 4.5 to about 6, about 4.5 to about 5.5 or about 5.

[0069] In some embodiments, the pH of the de-flavoured alkaline water soluble hemp protein extract is adjusted with an organic acid. In some embodiments, the acid is any suitable food grade acid, such as citric acid, hydrochloric acid or phosphoric acid, or a mixture thereof. [0070] In some embodiments, step d) of the method of the present application further comprises holding the pH of the de-flavoured alkaline water soluble hemp protein extract at its isoelectric point for about 15 minutes to about 45 minutes, or for example for about 30 minutes.

[0071] In some embodiments, the hemp protein product of step d) is collected using a centrifuge. For example, the centrifuge is a desludger centrifuge.

[0072] In some embodiments, the hemp protein product from step e) is pasteurized using a jet cooker.

[0073] In some embodiments, the hemp protein product from step e) is pasteurized at about 100°C to about 150°C for about 5 seconds to about 25 seconds, for example, at 120°C for about 15 seconds.

[0074] In some embodiments, the hemp protein product from step e) is optionally neutralized prior to being pasteurized.

[0075] In some embodiments, the hemp protein product from step e) is optionally adjusted to about 5% solids to about 20% solids prior to being pasteurized. In some embodiments, the hemp protein product is adjusted to about 10% solids prior to being pasteurized.

[0076] In some embodiments, the hemp protein product from step f) is flash cooled to about 50°C to about 60°C. In some embodiments, the flash cooling is performed under vacuum. In some embodiments, performing the flash cooling removes greater amounts of volatile flavour components.

[0077] In some embodiments, the hemp protein product from step g) is dried using a spray drier.

III. Protein Products of the Present Application and Uses thereof

[0078] In another aspect, the present application includes a pulse protein product produced by a method disclosed herein.

[0079] In some embodiments, the pulse protein product has a protein content of about 70% to about 95% on a dry weight basis. In some embodiments, the protein content is about 80%, about 85%, about 90% or about 95% (dry weight%). [0080] In some embodiments, the pulse protein product has a sodium level of about 15200 pg/g to about 16000 pg/g.

[0081] In some embodiments, the pulse protein product has a total microbial count of less than about 100,000 cfu/g. In some embodiments, the total microbial count is less than about 5000 cfu/g. In some embodiments, the total microbial count is less than about 1000 cfu/g.

[0082] In some embodiments, the pulse protein product has a protein dispersibility index of greater than about 80%.

[0083] In some embodiments, the pulse protein product has a water solubility of greater than about 80% at neutral pH.

[0084] In some embodiments, the pulse protein product has a Hunterlab™ L (lightness) value of about 80 to about 85. In some embodiments, the Hunterlab L (lightness) value is about 83 to about 84.

[0085] In some embodiments, the pulse protein product is bland tasting. For example, the pulse protein product is substantially free of pea, bean and/or other vegetable flavours.

[0086] In some embodiments, the pulse protein product has a water hydration capacity (WHC) of about 1.0 g/g to about 3.0 g/g. In some embodiments, the water hydration capacity is about 1.8 g/g to about 2.3 g/g. In some embodiments, the water hydration/holding capacity is determined using the method of Toews and Wang (2013) and Wang et al (2017). (1 ,2) Therefore, in some embodiments, 1 g of protein samples are (Wi, accurate to 1 mg) weighed into culture test tubes. The test tubes with samples and filter cloth are then put in a syringe barrel, and the weight of the syringe assembly is recorded (W2). Water, such as Milli-Q™ water, is added into the test tube and a stirring rod is used to stir the protein mixture until the mixture is fully wet and saturated with water. The mixture is stirred for another minute. The stirring rod is wiped with the filter cloth and the filter cloth placed at the end of the test tube. The test tube is then put upside down into the syringe barrel. The syringe barrel is put into a 50ml_ centrifuge tube for centrifugation at room temperature (21-23 °C) at 300 g for 10 min. There is about 0.05 - 0.2 mL liquid left in the centrifuge tube after centrifugation. The syringe assembly is weighed (W3). Water holding capacity is calculated using Eq 1. % WHC (g H₂0/g sample, dry matter)

where,

Wi = weight of sample before water addition (g);

W₂ = weight of syringe assembly (g);

W3 = weight of syringe assembly after centrifugation; me = initial moisture content of (5) of sample.

In some embodiments, measurements are done in duplicate.

[0087] In some embodiments, the pulse protein product has an oil holding capacity (OHC) of about 2.5 g/g to about 4 g/g. In some embodiments, the oil holding capacity is about 2.5 g/g to about 3.7 g/g. In some embodiments, the oil holding capacity of the pulse protein product is determined using the method of Stone et al. (2015). (3) Therefore in some embodiments, 0.5 g of protein is suspended in 5 g of canola oil in a 50 mL centrifuge tube. Each centrifuge tube is vortexed (e.g. VWR™ Vortex Mixer, VWR International, Mississauga, Canada) for 10 s every 5 min on maximum speed (speed 10). After 30 min, samples are centrifuged at room temperature (e.g. 21-23 °C) at 1000 g for 15 min., and the supernatant is discarded. OHC is calculated using Eq 2.

In some embodiments, the measurements are done in duplicate.

[0088] In some embodiments, the pulse protein product has a foam capacity (FC) of about 160% to about 230%. In some embodiments, the foam capacity is about 165%. In some embodiments, the foam capacity is about 190%. In some embodiments, the foam capacity is about 200% to about 220%.

[0089] In some embodiments, the pulse protein product has a foam stability (FS) of about 60% to about 80%, or about 70% to about 76%. In some embodiments, the pulse protein product has an emulsion stability of about 85% to about 95%m or about 90% to about 95%.

[0090] In some embodiments, FC and FS are determined using the method of Liu et al. (2010). (4) Therefore, in some embodiments, each protein is dissolved in water, for example Milli-Q water, to reach 1.00% (w/w) protein solution followed by adjusting pH to 7 (using 0.1 N NaOH). Protein solution pH is re-adjusted to pH 7.0 after stirring overnight at room temperature (21-23 °C). 15 mL (Vn) of protein solution is transferred into a 400 mL glass beaker (inner diameter = 69 mm; height = 127 mm; as measured by a digital caliper) and foamed using, for example, an Omni Macro™ homogenizer (Omni International, Marietta, GA, USA) with a 20mm saw tooth generating probe positioning slightly below the air-water interface for 5 min. Foaming starts at speed 3 followed by half unit increment in every 15 seconds till speed 4. The foam is immediately transferred to a 50 mL graduated cylinder after homogenization. Foam volume was recorded (Vfi), and the remaining foam was recorded (Vft) after 30 min. FC and FS were determined using Eq 3 & 4, respectively.

%FS = — X 100% (Eq.4) vfi

In some embodiments, the measurements are done in duplicate.

[0091] In another aspect, the present application includes a use of the pulse protein product of the present application to prepare a food and/or health product.

[0092] In another aspect, the present application includes a food and/or health product comprising the pulse protein product of the present application.

[0093] In some embodiments, the food and/or health product is selected from a beverage, a plant-based protein food product, and a protein dietary supplement.

[0094] In another aspect, the present application includes a hemp protein product produced by a method disclosed herein.

[0095] In some embodiments, the hemp protein product has a protein content of about 70% to about 95% on a dry weight basis. In some embodiments, the protein content is about 80%, about 85%, about 90% or about 95% (dry weight%).

[0096] In another aspect, the present application includes a use of the hemp protein product of the present application to prepare a food and/or health product.

[0097] In another aspect, the present application includes a food and/or health product comprising the hemp protein product of the present application. [0098] In some embodiments, the food and/or health product is selected from a beverage, a plant-based protein food product, and a protein dietary supplement.

EXAMPLES

[0099] The following non-limiting examples are illustrative of the present application:

Example 1 : Pulse protein production

A. Functionality Methods a. Water hydration capacity

[00100] Water holding capacity (WHC) was determined according to Toews and Wang (2013) and Wang et al (2017). (1 ,2) 1 g of sample (Wi, accurate to 1 mg) was weighted into each culture test. The test tube with samples and filter cloth were then put in a syringe barrel, and the weight of the syringe assembly was recorded (W2). Milli-Q™ water was added into the test tube and a stirring rod was used to stir the protein mixture until the mixture was fully wet and saturated with water. The mixture was stirred for another minute. The stirring rod was wiped with the filter cloth and the filter cloth placed at the end of the test tube. The test tube was then put upside down into the syringe barrel. The syringe barrel was put into a 50m L centrifuge tube for centrifugation at room temperature (21-23 °C) at 300 g for 10 min. There was about 0.05 mL - 0.2 mL liquid left in the centrifuge tube after centrifugation. The syringe assembly was weighed (W3). Water holding capacity was calculated using Eq 1.

% WHC (g H₂0/g sample, dry matter) ⁽¹ >

Where,

Wi = weight of sample before water addition (g);

W2 = weight of syringe assembly (g);

Measurements were done in duplicate. b. Oil holding capacity [00101 ] Oil holding capacity (OHC) was determined according to Stone et al. (1995) (3) by suspending 0.5 g of protein in 5 g of canola oil (purchased from local market) in a 50 mL centrifuge tube. Each centrifuge tube was vortexed (VWR™ Vortex Mixer, VWR International, Mississauga, Canada) for 10 s every 5 min on maximum speed (speed 10). After 30 min, samples were centrifuged at room temperature (21-23 °C) at 1000 g for 15 min., and the supernatant was discarded. OHC was calculated using Eq 2.

Measurements were done in duplicate. c. Foam capacity and stability

[00102] Foam capacity (FC) and foam stability (FS) were determined according to Liu et al. (2010). (4) Each protein was dissolved in Milli-Q water to reach 1.00% (w/w) protein solution followed by adjusting pH to 7 (using 0.1 N NaOH). Protein solution pH was re-adjusted to pH 7.0 after stirring overnight at room temperature (21-23 °C). 15 mL (Vii) of protein solution was transferred into a 400 mL glass beaker (inner diameter = 69 mm; height = 127 mm; as measured by a digital caliper) and foamed using an Omni Macro™ homogenizer (Omni International, Marietta, GA, USA) with a 20mm saw tooth generating probe positioning slightly below the air-water interface for 5 min. Foaming started at speed 3 followed by half unit increment in every 15 seconds till speed 4. The foam was immediately transferred to a 50 mL graduated cylinder after homogenization. Foam volume was recorded (Vfi), and the remaining foam was recorded (Vft) after 30 min. FC and FS were determined using Eq 3 & 4, respectively.

Measurements were done in duplicate. d. Emulsion stability

[00103] Emulsion stability (ES) was determined according to Stone and Nickerson (2012) (5) with a 1 .00% (w/w) protein solution as prepared for FC/FS. ES was tested for a 50/50 oil-in-water emulsion (5 g oil/ 5 g aqueous solution) using canola oil (purchased from local market). Emulsions were homogenized (Omni International™, Inc., Marietta, GA, USA) for 5 min at speed 4 with a 20 mm saw tooth generating probe with the position at the oil-water interface in 50 ml_ plastic centrifuge tubes. 10 mL of the emulsion was transferred to a 10 mL graduated cylinder (inner diameter = 10.80 mm; height = 100.24 mm; as measured by a digital caliper) and allowed to separate for 30 min. ES was determined using Eq 5, where VB and VA are the volume of the aqueous (or serum layer) before emulsification (5.0 mL) and after drainage at each time point, respectively.

Measurements were done in duplicate. e. Solubility

[00104] A protein solution (1 %, w/w) using each protein product was prepared in 0.1 M NaCI and the pH of a weighed aliquot (~18 g) taken from this solution for solubility testing was adjusted to pH 2, 4, 5, 7, or 10 using either 0.1 M HCI or 0.1 M NaOH. All solutions after adjusting pH were brought to 20 g with 0.1 M NaCI. Solutions were vortexed every 15 minute interval for a total of 1 hour at room temperature (18-25°C) and centrifuged at 9100 x g for 10 min at 22°C. Total weight of the supernatant was recorded. Protein content of the original sample and supernatant was determined using the LECO instrument (Nx 6.25). The % protein solubility for each solution at different pH was calculated by dividing the total protein content of the supernatant by the total protein content of the original sample aliquot used. f. Protein dispersibility index

[00105] The American Oil Chemists’ Society (AOCS) Official method Ba 10-65 method was used in measuring the protein dispersibility index (PDI) of final protein products.

B. Production of Pea, Fava beans, and Lentil Protein Products

[00106] Proteins from red lentil and fava bean flour (was extracted in water at ta 1 :10 flour: water ratio at pH 9.5 (adjusted using 50% NaOH) at a temperature of 18°C for 1 h.

Similar conditions were also used for extraction of yellow pea protein except the extraction pH was 9.0. Insoluble material was removed using a decanter centrifuge and discarded.

The supernatant was then passed through the HP20 resin (1 :~120-130 ratio of resin volume: protein extract volume, and at about 500 kg/h flow rate), and then IEP by adjusting the pH to 4.5 using 50% citric acid and held for 0.5 h. The precipitated protein was then collected using a desludger centrifuge, neutralized to pH 7 using 50% NaOH. The slurry was then adjusted to 10% solids, pasteurized using a jet cooker at 120°C for 15 seconds, followed by flash cooling at 50-60°C, and then spray dried to yield a product. Controls for both pea and fava bean were prepared without the adsorption resin treatment, jet cooking and flash cooling using a benchtop spray drier.

C. Properties of Lentil Protein Products

[00107] Production of lentil protein product using the above-described method yielded -14% mass recovery with products with protein contents of -80% on a dry weight basis (Table 1). The lentil protein products had sodium levels ranging from 15,200 to 16,600 pg/g and total plate counts <400 cfu/g. The control lentil protein product sample was light red in colour, whereas the addition of jet cooking/flash cooling produced product that was more beige in colour shown by a slight increase in the Hunterlab™ L (lightness) value from 83 to 84. All products showed good functionality and did not vary significantly between treatments (T able 1 ). Protein dispersibility index, which is a measure of how well the product goes into solution were all >89%. Solubility followed a typical pH-dependent profile where minimum solubility occurred at pH 5, which was close to the protein’s isoelectric point. Solubility at pH 5 ranged between 24% and 30%. At pH 3, solubility of the control was 59% whereas the treated sample was slightly lower at 44%. At neutral pH, solubility was at 65% and 87% for the control and treated lentil protein product, respectively. Water hydration and oil holding capacities ranged between 1.8 g/g -2.28 g/g and 3.23 g/g -3.70 g/g, respectively. Foam capacity and stability ranged between 207%- 214% and 71 %-76%, respectively, whereas emulsion stability ranged between 92%-94%.

D. Properties of Pea and Fava Bean Protein Products

[00108] Pea and fava bean protein products were produced using the above- described method. Percent mass yield and protein levels (dry weight basis) were found to be 15.0% and 80.4%, respectively for yellow pea, and 21.0% and 86.8%, respectively for fava bean (Table 1). All products produced with the above-described method carried low microbial counts (<140 cfu/g). Control samples were produced using a benchtop spray drier to produce products with protein levels of 89.7% and 93.1 % for yellow pea and fava bean, respectively (Table 1). All products produced were yellow in colour. Solubility for all products followed a typical pH-dependent profile, where minimum solubility occurred at pH 5, which was near the pi of the protein (~pH 4.5). For yellow pea, solubility of the control sample relative to the one processed on the pilot scale was greater at pH 3 and 7, but lower at pH 5. For instance, solubility at pH 3, 5 and 7 was 73%, 3%, and 80%, respectively for the control, and 46%, 25% and 51%, respectively for the protein product prepared using the above-described method (Table 1). In the case of fava bean, all solubility values were greater than control protein product. For instance, solubility at pH 3, 5 and 7 was 58%, 3% and 89%, respectively for the control, and 76%, 21% and 93%, respectively for the pilot plant prepared product (Table 1). Both water hydration and oil holding capacities (WHC and OHC respectively) were found to be larger for both pulse protein products when prepared at the pilot plant level vs. the control. Yellow pea products showed a WHC increase from 1.4 g/g to 2.0 g/g, whereas OHC increased from 2.4 g/g to 2.6 g/g. In the case of fava bean products, WHC increased from 1.4 g/g to 2.1 g/g, whereas OHC increased from 2.4 g/g to 3.1 g/g (Table 1). Foaming and emulsifying properties were similar between the control samples and those produced at the pilot scale.

Foam capacity and stability, and emulsion stability for pilot plant prepared yellow pea products were 188%, 70% and 93%, respectively. In contrast, for fava bean products, these values were 170%, 71% and 91%, respectively (Table 1).

Table 1 Pulse Protein Properties

E. Taste Testing

[00109] All products produced were taste tested and were bland tasting. Example 2: Pilot Plant Scale Hemp Protein Production

A. Hemp Seed Pressing

[00110] Pressing of 1500 kg hemp seeds produces about 1022 kg pressed cake and 225 kg of filtered oil. About 900 kg of milled hemp press cake was recovered after Hammer milling followed by pin milling (75%-80% through #50 US mesh) and was used for protein extraction.

B. Hemp Seed Protein Isolate Production [0100] Hemp flour produced in A above was mixed with soft water at 50°C and at 1 :5 (wt. flour/wt. water) ratio and collected into a tank through a powered-in-line mixer. Extraction was conducted by adjusting pH of the slurry to 11.0 using 50 % NaOH, and mixing for 1 hr at 50 °C. The pH was kept constant at 11.0 during the extraction period by adding 50 % NaOH as needed. The slurry was passed through a decanter (CA225-010, Westfalia Seperator AG, D-59302 Oelde, Postfach 3720) centrifuge and the protein extract liquid phase was collected in a separate tank from the solid phase. An additional washing of the collected solid phase was carried out by adding 2x water at 50°C, mixing for 1 h and recovering the second liquid phase by passing through the decanter. Light phase protein extract from the first and second decantations were combined. The combined light phases (protein extract) were then de-flavored by pumping though a bed of polystyrene/divinylbenzene polymeric resin (Diaion HP20, Mitubishi Corp., Tokyo, JP) at 1 : 120 bed volume to protein extract ratio. Following this treatment, the pH of the protein extract was adjusted to 5.0 using 85% phosphoric acid and held for 30 min. The slurry after holding was passed through a desludger centrifuge (CLARA 20 High Flow, Alfa Laval) and the solid phase protein product was collected into a tank. The total solids content of the protein product was adjusted 10% using soft water and the pH was adjusted to 7.0 using 50% potassium hydroxide. This slurry was pasteurized and further de- flavored by passing through a jet cooker (Pick SC2-1 , Pick Heaters Inc., West Bend, Indiana Ave, West Bend, Wl, USA) then into a reactor under vacuum to flash off additional flavor compounds. The resulting protein-rich slurry was spray dried (Komline Sanderson No. D-19, open-cycle co-current dryer, Cambrian Engineering, Mississauga, ON, Canada) at inlet and outlet temperatures of 170±5 °C and 70±5 °C, respectively.

E. Taste Testing

[00111] The resulting powdered hemp seed protein isolate was taste tested in a water-based beverage form at 10% (w/v) concentration and found to be bland tasting.

Example 3: De-flavoring Hemp Seed Protein with Different Polymeric Resins

A. Hemp seed protein processing

[00112] A 1.5 kg sample of hemp seed press cake produced from partially dehulled, pressed or milled hemp seeds was mixed with water at 1 :5 (w/w) ratio. The mixture was adjusted to pH 11.0 using 50% sodium hydroxide and protein was extracted at 50°C for 2 h with stirring. Following extraction, the liquid protein extract was recovered by centrifuging the mixture at 4,200 rpm for 10 minutes in a swinging bucket centrifuge. A total of 5,918 g of protein extract was recovered and separated into 3 samples of 1 ,972 g each. One sample was mixed with 50 ml_ of FPX66 (Dupont, Wilmington, DE) polymeric adsorbent resin beads in a beaker. The resin-protein extract mixture was agitated gently for 1 h then the resin was removed by filtration through a 100 mesh screen and the resulting protein solution was collected. A second 1 ,970 g sample of protein extract was treated the same except 50 ml_ of HP20 (Mitsubishi Corp., Tokyo, JP) polystyrene/divinylbenzene polymeric resin beads were used to remove the flavor compounds. A third sample was used a Control whereby no resin treatment was applied. All protein extract samples were then processed separately to recover the protein isolates. The pH of the protein extracts was adjusted to 5.0 with 85% phosphoric acid and held for 30 minutes. The samples were then centrifuged to recover the resulting precipitated protein and the protein was suspended in water adjusted to pH 7.0 using 50% potassium hydroxide and dried in a lab spray dryer (Buchii Labortechnik, Flawil, Switzerland) at 160°C inlet and 75°C outlet temperature.

B. Organoleptic Evaluation

[00113] Aqueous suspensions containing 10% protein were prepared from each of the Control and the 2 resin-treated protein isolates. Five panelists rated the samples on a scale of 1 to 5 whereby 1 represented “least” and 5 was “greatest” for nutty flavor, bitterness, grassy flavor, astringency and overall acceptability. The results are shown in Table 2 below. Overall, the Control sample, without any resin treatment was rated as the lowest acceptability score and was more bitter, astringent, nutty and was noted to exhibit a cardboard-like flavor and egg-like odor. Both resin treatments were effective in reducing off flavor and aroma notes from the hemp protein isolate.

Table 2: Sensory Evaluation Average Scores of Hemp Seed Protein Isolate Samples

Descriptor HP20 treated FPX66 treated Control

Nutty flavor 3.0 2.5 3.5

Bitterness 1.8 1.6 2.8

Grassy flavor 2.2 2.0 2.0

Astringency 2.1 1.8 2.9 Overall Acceptability 3.9 4.2 2.8

[00114] While the present application has been described with reference to examples, it is to be understood that the scope of the claims should not be limited by the embodiments set forth in the examples, but should be given the broadest interpretation consistent with the description as a whole.

[00115] All publications, patents and patent disclosures are herein incorporated by reference in their entirety to the same extent as if each individual publication, patent or patent disclosure was specifically and individually indicated to be incorporated by reference in its entirety. Where a term in the present application is found to be defined differently in a document incorporated herein by reference, the definition provided herein is to serve as the definition for the term.

FULL CITATIONS OF REFERENCED DOCUMENTS

1. Toews, R., & Wang, N. (2013). Physicochemical and functional properties of protein concentrates from pulses. Food Research International, 52, 445-451.

2. Wang, N., Wood, J.A., Panozzo, J.F., Arganosoa, G.C., Hall, C, Chen, L, Singh, M. and Nickerson, M.T. (2017). AACCI approved methods technical committee report: Collaborative study on a method for determining the water holding capacity of pulse flours and their protein materials (AACCI Method 56-37.01 ). Cereal Foods World, 62, 227-230.

3. Stone, A. K., Avramenko, N. A., Warkentin, T. D., & Nickerson, M. T. (2015). Functional properties of protein isolates from different pea cultivars. Food Science

& Biotechnology, 24, 827- 833.

4. Liu, S., Elmer, C., Low, N.H. and Nickerson, M.T. (2010). Effect of pH on the functional behavior of pea protein isolate-gum Arabic complexes, Food Research International, 43, 489-495. 5. Stone, A. K. and Nickerson, M.T. (2012). Formation and functionality of whey protein isolate - (kappa-, iota-, and lambda-type) carrageenan electrostatic complexes. Food Hydrocolloids, 27, 271-277.

Claims

CLAIMS:

1 . A method of producing a pulse protein product comprising a) extracting a pulse protein source with an aqueous solution having a pH greater than about 8.5 to obtain an alkaline water soluble pulse protein extract and residual pulse protein source; b) separating the alkaline water soluble pulse protein extract from the residual pulse protein source; c) passing the alkaline water soluble pulse protein extract through a non-polar adsorption resin that removes flavouring compounds to obtain a de-flavoured alkaline water soluble pulse protein extract; d) adjusting the pH of the alkaline deflavoured water soluble pulse protein extract to reach its isoelectric point to precipitate the pulse protein product; e) optionally collecting the pulse protein product from d); f) optionally pasteurizing the pulse protein product from e); g) optionally flash cooling the pasteurized pulse protein product from f); and h) optionally spray drying the flash cooled pulse protein product from g).

2. The method of claim 1 , wherein the pulse protein source is selected from lentil, beans, peas and combinations thereof.

3. The method of claim 1 or 2, wherein the pulse protein source is ground and/or milled pulse.

4. The method of any one of claims 1 to 3, wherein the pulse protein source is pulse flour.

5. The method of any one of claims 1 to 4, wherein the ratio of the pulse protein source to the aqueous solution is about 1 :4 to about 1 :20.

6. The method of claim 5, wherein the ratio of the pulse protein source to the aqueous solution is about 1 :10.

7. The method of any one of claims 1 to 5, wherein the extracting of the pulse protein source is at a temperature of about 10°C to about 55°C.

8. The method of claim 7, wherein the temperature is about 15°C to about 55°C, or about 50°C.

9. The method of any one of claims 1 to 8, wherein the pH of the aqueous solution is about 8.5 to about 12.

10. The method of any one of claims 1 to 9, wherein the alkaline water soluble pulse protein extract is separated from the residual protein source using a decanter centrifuge.

11. The method of any one of claims 1 to 10, wherein the non-polar adsorption resin comprises porous particles having an average pore diameter between about 0.2 mm to about 1.5 mm.

12. The method of claims 11 , wherein the average pore diameter of the porous particles is about 0.5 mm.

13. The method of any one of claims 1 to 12, wherein the non-polar adsorption resin comprises a polyaromatic polymer, a polyaromatic co-polymer, a polymethylacrylate polymer or a polymethylacrylate co-polymer.

14. The method of claim 13, wherein the polyaromatic polymer or polyaromatic co polymer is polystyrene, polydivinylbenzene, or polystyrene-divinylbenzene co-polymer.

15. The method of any one of claims 1 to 14, wherein the alkaline water soluble pulse protein extract is passed through the non-polar adsorption resin with a flow rate of about 200 kg/h to about 700 kg/h.

16. The method of claim 15, wherein the flow rate is about 500 kg/h.

17. The method of any one of claims 1 to 16, wherein in step c), the ratio of resin volume to water soluble pulse protein extract volume is about 1 : 100 to about 1 :200.

18. The method of any one of claims 1 to 17, wherein the isoelectric point of the de- flavoured water soluble pulse protein extract is about pH 4 to about 6.

19. The method of any one of claims 1 to 18, wherein the pH of the de-flavoured alkaline water soluble pulse protein extract is adjusted with citric acid.

20. The method of any one of claims 1 to 19, wherein step d) further comprises holding the pH of the de-flavoured alkaline water soluble pulse protein extract at its isoelectric point for about 15 minutes to about 45 minutes.

21. The method of any one of claims 1 to 20, wherein the pulse protein product of step d) is collected using a centrifuge.

22. The method of claim 21 , wherein the centrifuge is a desludger centrifuge.

23. The method of any one of claims 1 to 22, wherein the pulse protein product from step e) is pasteurized using a jet cooker.

24. The method of any one of claims 1 to 23, wherein the pulse protein product from step e) is pasteurized at about 100°C to about 150°C for about 5 seconds to about 25 seconds.

25. The method of any one of claims 1 to 24, wherein the pulse protein product from step e) is optionally neutralized prior to being pasteurized.

26. The method of any one of claims 1 to 25, wherein the pulse protein product from step e) is optionally adjusted to about 5% solids to about 20% solids prior to being pasteurized.

27. The method of any one of claims 1 to 26, wherein the pulse protein product from step f) is flash cooled to about 50°C to about 60°C and the flash cooling is optionally performed under vacuum.

28. The method of any one of claims 1 to 27, wherein the pulse protein product from step g) is spray dried.

29. A pulse protein product prepared by the method of any one of claims 1 to 28.

30. The pulse protein product of claim 29, having a protein content of about 70% to about 95% on a dry weight basis.

31. The pulse protein product of claim 30, wherein the protein content is about 80% to about 95%.

32. The pulse protein product of any one of claims 29 to 31 , having a sodium level of about 15200 pg/g to about 16000 pg/g.

33. The pulse protein product of any one of claims 29 to 32, having a protein dispersibility index of greater than about 80%.

34. The pulse protein product of any one of claims 29 to 33, having a water solubility of greater than about 80% at neutral pH.

35. The pulse protein product of any one of claims 29 to 34, having a Hunterlab L (lightness) value of about 80 to about 85.

36. The pulse protein product of claim 35, wherein the Hunterlab L (lightness) value is about 83 to about 84.

37. The pulse protein product of any one of claims 29 to 36, having a water hydration capacity of about 1.0 g/g to about 3.0 g/g.

38. The pulse protein product of claim 37, wherein the water hydration capacity is about 1.8 g/g to about 2.3 g/g.

39. The pulse protein product of any one of claims 29 to 38, having an oil holding capacity of about 2.5 g/g to about 4 g/g.

40. The pulse protein product of claim 39, wherein the oil holding capacity is about 2.5 g/g to about 3.7 g/g.

41. The pulse protein product of any one of claims 29 to 40, having a foam capacity of about 160% to about 230%.

42. The pulse protein product of claim 41 , wherein the foam capacity is about 165%.

43. The pulse protein product of claim 41 , wherein the foam capacity is about 190%.

44. The pulse protein product of claim 41 , wherein the foam capacity is about 200% to about 220%.

45. The pulse protein product of any one of claims 29 to 44, having stability of about 60% to about 80%.

46. The pulse protein product of claim 45, wherein the stability is about 70% to about 76%.

47. The pulse protein product of any one of claims 29 to 46, having an emulsion stability of about 85% to about 95%.

48. The pulse protein product of claim 47, wherein the emulsion stability is about 90% to about 95%.

49. The pulse protein product of any one of claims 29 to 48, wherein the pulse protein product is bland tasting.

50. Use of the pulse protein product of any one of claims 29 to 49 to prepara a food and/or health product.

51. The use of claim 50, wherein the food and/or health product is selected from a beverage, a plant-based protein food product, and a protein dietary supplement.

52. A food and/or health product comprising the pulse protein product of any one of claims 29 to 49.

53. The food and/or health product of claim 52, wherein the food and/or health product is selected from a beverage, a plant-based protein food product, and a protein dietary supplement.

54. A method of producing a hemp protein product comprising: a) extracting a hemp protein source with an aqueous solution having a pH greater than about 8.5 to obtain an alkaline water soluble pulse protein extract and residual hemp protein source; b) separating the alkaline water soluble hemp protein extract from the residual hemp protein source; c) passing the alkaline water soluble hemp protein extract through a non-polar adsorption resin that removes flavouring compounds to obtain a de-flavoured alkaline water soluble hemp protein extract; d) adjusting the pH of the de-flavoured alkaline water soluble hemp protein extract to reach its isoelectric point to precipitate the hemp protein product; e) optionally collecting the hemp protein product from d); f) optionally pasteurizing the hemp protein product from e); g) optionally flash cooling the pasteurized hemp protein product from f); and h) optionally spray drying the flash cooled pulse protein product from g).

55. The method of claim 54, wherein the hemp protein source is any species of the Cannabis plant genus, including, but not limited to Cannabis sativa, Cannabis indica , and Cannabis ruderalis.

56. The method of claim 54 or 55, wherein the hemp protein source is hemp seed, stalk and/or leaves.

57. The method of claim 56, wherein the hemp protein source is hemp seed, optionally de-hulled hemp seed, milled hemp seed or flaked hemp seed, optionally a milled hemp seed press cake from whole or dehulled hemp seed.

58. The method of claim 57, wherein the hemp protein source is defatted hemp seed.

59. The method of claim 58, wherein the hemp seed is defatted using expeller pressing, cold pressing or by producing expanded pellets produced using expander pelletizers followed by extraction of the oil using an organic solvent.

60. The method of claim 57, wherein the hemp seed source is non-defatted hemp protein source and the method further includes a step of fat removal during the protein extraction step a.

61. A hemp protein product prepared by the method of any one of claims 54 to 60.

62. Use of the hemp protein product of claim 61 to prepare a food and/or health product.

63. The use of claim 62, wherein the food and/or health product is selected from a beverage, a plant-based protein food product, and a protein dietary supplement.

64. A food and/or health product comprising the hemp protein product of claim 61 .

65. The food and/or health product of claim 64, wherein the food and/or health product is selected from a beverage, a plant-based protein food product, and a protein dietary supplement.