CN114680226B - Gluten protein treatment method and application - Google Patents
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Classifications
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- A—HUMAN NECESSITIES
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
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- A23G9/00—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor
- A23G9/32—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor characterised by the composition containing organic or inorganic compounds
- A23G9/38—Frozen sweets, e.g. ice confectionery, ice-cream; Mixtures therefor characterised by the composition containing organic or inorganic compounds containing peptides or proteins
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
- A23L2/38—Other non-alcoholic beverages
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- B—PERFORMING OPERATIONS; TRANSPORTING
- B65—CONVEYING; PACKING; STORING; HANDLING THIN OR FILAMENTARY MATERIAL
- B65D—CONTAINERS FOR STORAGE OR TRANSPORT OF ARTICLES OR MATERIALS, e.g. BAGS, BARRELS, BOTTLES, BOXES, CANS, CARTONS, CRATES, DRUMS, JARS, TANKS, HOPPERS, FORWARDING CONTAINERS; ACCESSORIES, CLOSURES, OR FITTINGS THEREFOR; PACKAGING ELEMENTS; PACKAGES
- B65D65/00—Wrappers or flexible covers; Packaging materials of special type or form
- B65D65/38—Packaging materials of special type or form
- B65D65/46—Applications of disintegrable, dissolvable or edible materials
- B65D65/463—Edible packaging materials
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A40/00—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production
- Y02A40/90—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production in food processing or handling, e.g. food conservation
Landscapes
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- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Health & Medical Sciences (AREA)
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- Inorganic Chemistry (AREA)
- Biochemistry (AREA)
- Mechanical Engineering (AREA)
- Peptides Or Proteins (AREA)
Abstract
The application provides a treatment method of gluten, which aims at improving the solubility and emulsification characteristics of the gluten. After the gluten protein solution is subjected to heat treatment and pH circulating treatment, disulfide bonds of gluten protein molecules are broken, the content of free sulfhydryl groups is increased, the surface hydrophobicity is increased, the particle size is reduced, and the solubility and the emulsification property of the gluten protein are obviously improved. Thereby providing a solution for expanding the application market of gluten proteins.
Description
Technical Field
The application relates to the field of food processing, in particular to a gluten protein processing method and application thereof.
Background
Wheat gluten, commonly known as Wheat Gluten (WG), is a kind of high quality plant protein commonly found in life, and Wheat gluten has a protein content of up to 70% -80%, and the main components are Glutenin with larger molecular weight (Glutenin) and Gliadin with smaller molecular weight (Gliadin). Gliadin molecules appear to be nonpolar, primarily because of the disulfide bonds present within their molecules; whereas the wheat Gu Rong protein has both intermolecular disulfide bonds and intramolecular disulfide bonds, the formation of intermolecular disulfide bonds is due to the association of protein subunits by interactions.
Wet gluten (Wet gluten) refers to the dispersion of gluten in water in which starch is dissolved and gluten molecules interact with the water to form protein aggregates having a unique network structure. Wet gluten has excellent extensibility, viscoelasticity, water absorption, film forming and other characteristics, and increases the application possibility of gluten protein in food and other industries. But cannot be used as a good emulsifier in the food and other industries due to the poor functional properties of gluten proteins such as solubility and emulsifying properties. Therefore, in order to increase the application market of the gluten, various different requirements in the food industry and other industries are satisfied, and a proper method is required to be searched for modifying the gluten so as to improve the emulsifying property of the gluten.
Wheat gluten is poorly water-soluble in a neutral environment, mainly in the form of aggregates of gluten with a relatively large molecular weight, which is mainly due to the presence of a large number of non-polar amino acid residues (proline, leucine, etc.) and non-dissociable polar glutamine residues in the wheat gluten molecule. When gluten proteins interact with water molecules, a special gluten three-dimensional network structure is formed, and unique structural and functional characteristics are endowed to the gluten proteins. Gluten proteins contain a high number of disulfide bonds, two types of disulfide bonds, intramolecular and intermolecular disulfide bonds, respectively. The viscoelasticity and extensibility of the gluten are respectively endowed by glutenin and gliadin, wherein the glutenin forms protein polymers with different molecular weights, and the glutenin is intertwined into fiber shape, has intermolecular disulfide bonds and intramolecular disulfide bonds, can resist deformation to a certain degree, and endows the gluten with viscoelasticity. Gliadin has no intermolecular disulfide bond, so that the gliadin has strong fluidity and certain extensibility. The structural and functional properties of gluten proteins may also be altered by changes in external factors. When the external environment changes, such as pH and temperature changes, a certain amount of disulfide bonds can be broken, and free sulfhydryl groups are generated. Solubility can be enhanced by disrupting the hydrogen bonding and hydrophobic interactions between protein molecules, or by modifying functional groups of the amino acid side chains of the protein. The various functional properties of gluten depend on the solubility of gluten. Thus, upon a change in the solubility of gluten, the functional properties of the protein change, thereby affecting the application of gluten in the food field. So improving the solubility and the emulsifying property is an important content for expanding the gluten application market.
Three techniques for improving the emulsifying property through plant protein modification and wide application exist at present: physical, enzymatic, chemical methods.
The physical modification is mainly known in the modes of a wet heat method, a microwave method, an ultra-high pressure method, an ultrasonic method, extrusion treatment and the like. These ways to increase the emulsifying properties of gluten proteins are mainly due to the fact that some thermal, electrical or mechanical energy changes that they produce can alter the molecular structure and intermolecular aggregation of proteins, which in turn affect their functional properties. Wet heat treatment and microwave treatment are accepted by the general public as physical methods for improving the emulsifying properties of gluten. The enzyme method is to select proper enzyme to act on different molecular structures of the gluten protein to change the molecular conformation of the protein, so that various functional properties such as solubility and emulsifying property of the gluten protein are greatly changed. Hydrolytic modification and non-hydrolytic modification are the main pathways for enzymatically modifying wheat gluten.
Functional groups such as sulfhydryl groups, carboxylic acid groups, amino groups, amide groups and the like occupy a relatively large amount in wheat gluten protein, and the amide groups have a relatively large content compared with other functional groups, so that the functional groups have a relatively large influence on the structure and functional characteristics of the protein. The more common chemical modification methods of proteins are acylation, phosphorylation, glycosylation, deamidation, covalent cross-linking, and the like. Functional groups of the wheat gluten protein are increased or reduced by a chemical method, so that the protein emulsifying property is improved.
Gluten protein has high nutritive value as a high-quality plant protein, but has unsatisfactory functional characteristics due to poor water solubility of the gluten protein due to the structural characteristics of the gluten protein, so that the application of the gluten protein in food and other industries is hindered. The application aims to find a modification method suitable for gluten, which changes the internal structure of gluten molecules and improves the functional characteristics of the gluten such as solubility, emulsibility and the like.
The pH circulation combined with heat treatment can remarkably improve the solubility and emulsification characteristics of the gluten, and primarily solves the problem that the gluten cannot be better applied to food and other industries due to poor solubility and emulsification. Compared with animal proteins and other plant proteins, the gluten protein has the advantages of wide sources and low cost, but the gluten protein has complex internal bonds (hydrophobic bonds, hydrogen bonds, disulfide bonds and the like) and complex network structures, so that the gluten protein has extremely low solubility and severely restricts the wide application in food systems. The method can effectively improve the solubility and the emulsifying property of the gluten, is hopeful to expand the application range of the gluten, and is applied to systems such as protein drinks, edible packaging films, vegetable fat powder, ice cream, plant meat and the like.
Disclosure of Invention
The technical problem solved by the application is that the gluten protein is taken as a high-quality plant protein, has higher nutritive value, but has unsatisfactory functional characteristics due to poor water solubility of the gluten protein, and prevents the gluten protein from being applied to food and other industries. The application aims to find a modification method suitable for gluten, which changes the internal structure of gluten molecules and improves the functional characteristics of the gluten such as solubility, emulsibility and the like.
In order to achieve the above object, the present application provides a method for processing gluten protein, comprising the following steps:
step 1, dissolving gluten in distilled water at 20-30 ℃ to prepare a gluten water solution;
step 2, adopting pH circulation and heat treatment to the gluten protein water system, specifically, firstly adjusting the gluten protein water system to be alkaline by using an alkaline solution, stirring after heating treatment, and then adjusting the gluten protein water system to be neutral by using an acidic solution, and collecting the gluten protein water system after treatment;
and 3, centrifuging the collected gluten protein water system, taking supernatant, and freeze-drying to obtain a gluten protein sample.
In one embodiment, the heat treatment is stirred at 40 ℃ to 80 ℃.
In one embodiment, the concentration of the gluten protein water system is 5-50mg/mL.
In one embodiment, the alkaline solution is NaOH solution, KOH solution.
In one embodiment, the acidic solution is HCl solution, H 2 SO 4 A solution.
In one embodiment, the pH cycling in combination with heat treatment adjusts the gluten protein water system to alkaline in order to adjust the pH of the gluten protein water system to 11-12.
In one embodiment, the pH cycle in combination with heat treatment uses an acidic solution to adjust the gluten water system back to neutral in order to adjust the pH of the gluten water system to a value of 6.5-7.5.
In one embodiment, the centrifugation conditions are centrifugation at 70000 g for 10min at 20deg.C.
The application also provides an application of the treatment method in the field of food product treatment.
In one embodiment, the food product comprises: protein beverage, edible packaging film, vegetable fat powder, ice cream and vegetable meat.
Advantageous effects
The application provides a treatment method of gluten, which can effectively improve the solubility and emulsification characteristics of the gluten by combining pH circulation with heat treatment. At the heat treatment temperature of 80 ℃, the solubility and the emulsification property of the gluten protein solution with the concentration of 5mg/mL are obviously improved after the gluten protein solution is subjected to pH cyclic treatment. Wherein the solubility of the gluten protein is improved to about 70%, and the emulsifying activity and the emulsifying stability are respectively improved to 30.98m 2 /g and 54.08min.
The heat treatment and the pH circulating treatment mainly act on the molecular structure of the gluten so as to improve the solubility and the emulsifying property of the gluten. The heat treatment and the pH circulating treatment can extend the molecular structure of the gluten protein to a certain extent, expose hydrophobic groups in the molecules and increase the interaction force of the gluten protein molecules and water. Meanwhile, the heat treatment and the pH circulating treatment can also break intermolecular disulfide bonds to a certain extent to depolymerize the gluten macromolecular aggregates, so that the molecular particle size is reduced. Wherein, pH circulation can also increase the negative charge carried on the surface of protein molecules in the alkaline denaturation process, and increase the electrostatic repulsive force between protein molecules, so that gluten protein molecules are more stable and uniform in a dispersion system. The above structural changes can improve the solubility and emulsifying properties of the gluten.
Drawings
FIG. 1 solubility of gluten proteins under different treatments
FIG. 2 particle size of gluten proteins from different treatments
FIG. 3 emulsifying Activity and emulsion stability of gluten proteins under different treatments
FIG. 4 microscopic imaging of gluten proteins under different treatments
FIG. 5 free thiol content of gluten proteins from different treatments
FIG. 6 surface hydrophobicity of gluten proteins under different treatments
Detailed Description
The present application is further illustrated below in conjunction with specific embodiments, it being understood that these embodiments are meant to be illustrative of the application and not limiting the scope of the application, and that modifications of the application, which are equivalent to those skilled in the art to which the application pertains, fall within the scope of the application as defined in the appended claims after reading the application.
Example 1
Protein sample preparation:
at room temperature, the gluten protein is dissolved in distilled water to prepare a gluten protein water solution with the protein concentration of 5mg/mL, after being fully stirred,
wherein, gluten aqueous solution without any treatment was used as a control group. Taking three gluten protein aqueous solutions for heat treatment only: respectively performing heat treatment at 40deg.C, 60deg.C and 80deg.C for 30min, and stirring at room temperature for 1 hr; the pH was adjusted to 12.0 with 1M NaOH solution, wherein 3 gluten protein aqueous solutions were heat-treated at 40℃and 60℃and 80℃for 30min, respectively, stirred at room temperature for 1h, then adjusted to 7.0 with 1M HCl solution (pH cycling method), and stirring was continued at room temperature for 1h. Simultaneously, taking 3 gluten protein aqueous solutions, respectively carrying out heat treatment at 40 ℃,60 ℃ and 80 ℃ for 30min, and continuously stirring for 1h at room temperature. Centrifuging all the treated gluten protein solutions at 70000 g and 20 ℃ for 10min, pouring the supernatant into a culture dish, placing the culture dish in a refrigerator at-80 ℃ for prefreezing for 12h, and then freeze-drying for 48h, wherein the powder obtained by freeze-drying is the gluten protein sample and is used for measuring later indexes.
Embodiment two:
solubility determination
Pouring the centrifuged gluten supernatant into a culture dish, reserving the precipitate in a centrifuge tube, drying the precipitate in an oven at 55 ℃ overnight, weighing the centrifuge tube and the precipitate together after drying, subtracting the original centrifuge tube mass from the obtained mass to obtain the precipitate mass, and calculating the gluten solubility as solubility 1 according to the obtained gluten precipitate mass. After 48h of freeze-drying of the gluten supernatant, carefully taking out the gluten freeze-dried sample, weighing, and obtaining the gluten solubility of 2 according to the quality of the obtained gluten supernatant.
As shown in FIG. 1, the 9 treatments all had some effect on the solubility of the gluten. Wherein the heat treatment alone improves less the solubility enhancement of gluten than the control, but the solubility of gluten gradually increases as the heat treatment temperature increases. The heat-treated gluten combined with the pH12 shift treatment had a significant increase in the solubility of the gluten (p < 0.05) compared to the control and heat-treated gluten alone, again with increasing solubility with increasing temperature.
The solubility of the gluten after heat treatment and pH circulation treatment is obviously increased (p is less than 0.05) compared with the control group, and the solubility is obviously increased (p is less than 0.05) along with the rise of temperature, wherein the solubility of the gluten after 80 ℃ and pH circulation treatment is improved to about 70 percent.
Early experiments show that the pH circulation method is singly used for treatment at normal temperature, and the solubility of the gluten is not obviously improved. This demonstrates that the solubilization of gluten is significantly better (p < 0.05) with heat treatment combined with pH cycling than the addition of the improvement levels with heat treatment alone and pH cycling alone. As can be seen from the fifth example, this is because the heat treatment and the pH cycle treatment break the network structure of gluten protein with different bonds (hydrophobic bond, hydrogen bond, disulfide bond, etc.), and the two methods can promote each other by simultaneous treatment, thereby exerting a synergistic effect. Wherein the heat treatment temperature is 80 ℃ and the gluten protein solubilization effect is best when the heat treatment is combined with pH cyclic treatment.
Example III
Determination of the average particle size of the emulsion
The average particle diameter of protein molecules was measured, and a dynamic laser light scattering (DLS) was measured by selecting a laser particle diameter potential analyzer equipped with λ=633 nm He/Ne and setting the scattering angle to 173 °. The average particle size was measured by pipetting 1mL of different gluten sample solutions at a concentration of 5mg/mL into a cuvette (polystyrene) (refractive index 1.33) of special material with a pipette. Wherein the measurement temperature is set to 25+/-0.1 ℃ and the temperature is kept for 3min. Three replicates were run for each protein sample, each replicate was scanned three times and the final results averaged.
The size of the protein particle size has great influence on the structure and functional characteristics of the protein, and has important application value for improving the utilization rate of protein resources.
As shown in FIG. 2, the 9 treatments all had a certain effect on the average particle size of the gluten. Wherein the average particle size of the gluten protein heat treated alone is reduced (p < 0.05) compared with the control group, and the average particle size is gradually reduced with the rise of temperature; the average particle size of the gluten protein of the heat treatment combined with the pH12 shift treatment was significantly reduced (p < 0.05) and the average particle size was reduced with increasing temperature.
The average particle size of the gluten proteins treated by the heat treatment in combination with the pH cycling was significantly reduced (p < 0.05) compared to the control group, and the average particle size was reduced with increasing temperature. The average particle size of gluten after the treatment of 40 ℃,60 ℃ and 80 ℃ combined with pH circulation is respectively reduced to 1254.33nm, 1015.78nm and 912.10nm.
The results show that the pH value of the gluten protein solution in the control group is near the isoelectric point, and when the pH value is close to the isoelectric point of the protein, the electrostatic repulsive force among protein molecules is reduced due to the electrostatic shielding effect existing among charges; because of the hydrophobic interaction between molecules, the mutual attraction of protein molecules is enhanced, the protein molecules are aggregated, and the liquid drops have larger particle sizes and poorer solubility. When the gluten protein is heat treated, the grain size is found to be changed, which proves that the gluten protein is depolymerized and denatured to a certain extent in the heat treatment process, and the grain size of the protein molecules is reduced. In the alkaline denaturation process, the pH value of the gluten protein solution is increased to 12, the degree of deviation from isoelectric points is large, the negative charges carried on the surfaces of protein molecules are obviously increased, the electrostatic repulsive force among the gluten protein molecules is further increased, and meanwhile, the particle size of the protein molecules in the solution is obviously reduced, so that a uniform and stable dispersion system is formed. The smaller the particle size of the protein molecules, the more favorable the protein molecules form a more stable state in a dispersion system, and the better influence on the improvement of the emulsifying property is achieved.
Example IV
Determination of emulsion Properties
(1) Preparation of protein emulsions
And diluting gluten protein samples subjected to different treatments into a protein solution with the protein concentration of 5mg/mL by taking deionized water as a solvent, fully and uniformly vortex the gluten protein solution by using a vortex machine, taking 4mL of the gluten protein solution, respectively placing the gluten protein solution into a 10mL centrifuge tube, adding 1mL of peanut oil into the centrifuge tube, and dispersing the gluten protein solution for 2min by using a dispersing machine under the condition of 13500r/min after obvious water-oil layering phenomenon can be seen.
(2) Determination of protein emulsification Activity and emulsion stability
Adding 20 μL fresh emulsion accurately sucked by a pipette into 5mL 0.1% SDS solution, mixing uniformly by a vortex, sucking liquid at the bottom of a test tube (avoiding sucking foam into the pipette to prevent experimental error), placing into Dan Yingmin, measuring absorbance at 500nm, and recording as A 0 The method comprises the steps of carrying out a first treatment on the surface of the After the emulsion has been allowed to stand for 30 minutes, the liquid is again sucked up at a fixed location, as inThe absorbance at 500nm was measured and the reading was recorded as A 30 Three replicates were run with 0.1% SDS solution as a blank for each sample and the final results averaged. The Emulsification Activity Index (EAI) and Emulsification Stability Index (ESI) are calculated according to the following formulas:
EAI(m 2 /g)＝(2×T×A 0 ×N)/(C×Φ×10 4 )
ESI(min)＝30×A 0 /(A 0 -A 30 )
wherein: t=2.303, n: dilution factor, Φ: the ratio of the oil phase in the emulsion,
c: protein concentration (g/mL) in aqueous protein solution.
(3) Observing the microstructure of the emulsion
The microstructure of the emulsion and the emulsification effect can be observed more carefully after the dyeing treatment by using an inverted fluorescence microscope. To 5mL of freshly prepared emulsion, 20 μl of fluorescent dye (1% nile blue) accurately aspirated with a pipette was added, and the mixture was uniformly stained by appropriate shaking, 10 μl of emulsion was dropped onto the slide glass in a dark environment, the cover glass was covered, ensuring that no air bubbles were present between the slide glass and the cover glass, and a suitable objective magnification and light source were selected under an inverted fluorescent microscope for observation and photographing.
Each gluten sample was run in at least three replicates and the final results were presented as mean ± standard deviation. And calculating the average value and standard deviation of each group of data through Excel in WPS Office software. A one-way analysis of variance (ANOVA) and Duncan multi-range test was performed on each set of data using SPSS16.0 software to calculate whether there was significance between each set of averages. The results of each set of experiments were plotted using Origin 2019, and were presented primarily using a bar graph.
Emulsifying is an important functional property of gluten proteins, defined as the ability of water and fat to form emulsions, reflecting the ability of protein-protein, protein-fat to crosslink with each other. The intrinsic structure and composition of the protein have a great influence on the emulsifying properties. The two most commonly used indicators for evaluating protein emulsification properties are emulsification activity and emulsification stability.
Emulsifying Activity
The emulsifying activity is defined as the ability of protein to stabilize the oil-water interface in the process of accelerating oil-water mixing, i.e. the area of the oil-water interface where the protein can be stabilized per unit mass.
As shown in FIG. 3, the 9 treatment groups all had a certain effect on the emulsifying activity of the gluten. Wherein, compared with the control group, the gluten protein emulsifying activity of the independent heat treatment is increased, and the emulsifying activity is gradually increased along with the temperature rise, but the emulsifying activity is not changed significantly; the emulsifying activity of the gluten protein of the heat treatment combined with the pH12 shift treatment was significantly increased (p < 0.05) and increased with increasing temperature.
The emulsifying activity of the control group was 3.82m 2 And/g. The emulsifying activity of the gluten protein of the heat treatment combined with the pH cycle treatment was significantly increased (p < 0.05) compared with the control group, and the emulsifying activity was increased with the temperature rise. The gluten emulsifying activity of the gluten after being treated by the cycle of 40 ℃,60 ℃ and 80 ℃ and pH is respectively increased to 28.08m 2 /g、29.58m 2 /g、30.98m 2 /g。
The result shows that the emulsifying activity of the control group is poor, the pH value is near the isoelectric point, the surface of the gluten protein molecules is almost uncharged, the intermolecular electrostatic repulsive force is obviously reduced, and further, the protein molecules interact to form larger aggregates, the solubility is worst, so that the emulsifying activity is poor. The heat treatment is favorable for the movement and interaction between protein and water molecules, so that larger gluten protein aggregates are partially depolymerized, the solubility in water is increased, and the emulsifying activity is improved. In the alkaline denaturation process, when the pH value is far away from the isoelectric point, the surface charge of the gluten protein is obviously increased, the interaction force with surrounding groups is enhanced, the solubility is improved, and the emulsification activity is also increased.
Emulsion stability
Emulsion stability refers to the ability of protein as an emulsifier to maintain mutual non-separation after water and oil are mixed and to resist interference of external conditions, and the interfacial adsorption amount is a key index of emulsion stability.
As shown in FIG. 3, the 9 treatment groups all had a certain effect on the emulsion stability of the gluten. Wherein, compared with the control group, the gluten protein emulsion stability of the independent heat treatment is increased, and the emulsion stability is gradually increased along with the temperature rise, but the emulsion stability is not changed significantly; the heat treatment combined with pH12 shift treatment significantly increased the emulsion stability of the gluten (p < 0.05) and increased with increasing temperature.
The emulsion stability of the control group was 33.25min. The emulsion stability of the gluten proteins of the heat treatment combined with the pH cycling treatment was significantly increased (p < 0.05) compared to the control group, and increased with increasing temperature. The gluten protein emulsion stability after the treatment of the pH circulation at 40 ℃,60 ℃ and 80 ℃ is respectively increased to 47.67min,49.88min and 54.08min.
The result shows that the emulsion stability of the control group is poor because the gluten protein almost has no electrostatic charge when the external environment is close to the isoelectric point, the intermolecular electrostatic repulsion is small, the interaction of the gluten protein molecules further generates intermolecular aggregation, the oil drops can not be well combined with the protein molecules, the interfacial protein adsorption quantity is low, and the emulsion stability is poor. The reason why the heat treatment increases the emulsification stability of the gluten is that after the heat treatment, the molecular structure of the gluten is changed from compact to loose due to heat movement, and the hydrophobic groups of the protein molecules are fully exposed, so that the contact area with oil drops is increased, the adsorption of the gluten on an oil-water interface is favorably influenced, and the emulsification stability is increased. In the alkaline denaturation process, the pH value is greatly far away from the isoelectric point, the negative charge of gluten protein molecules is greatly increased, the intermolecular electrostatic repulsion is enhanced, emulsified particles are more dispersed, oil drops in the emulsion better interact with protein molecules, the adsorption capacity of interfacial proteins is improved, and the stability of the emulsion is improved.
Inverted fluorescent microscope
The microstructure of the oil-in-water emulsions of the different treatments of the following gluten proteins was observed by means of an inverted fluorescence microscope.
As can be seen from FIG. 4, the gluten emulsion prepared by the normal temperature treatment exhibits nonuniform larger droplets, and it can be confirmed that the gluten emulsion has poor emulsification properties and poor properties of dispersing and stabilizing oil droplets. In fig. 4, the gluten protein samples prepared by the treatments of (a), (b), (c), (d), (e), (f), (g), (h), (i), (j) are respectively 40 ℃,60 ℃,80 ℃, 40 ℃, pH cycle, 60 ℃,80 ℃, pH cycle, 40 ℃, pH12 shift, 60 ℃, pH12 shift, 80 ℃ pH12 shift, and as can be seen from fig. 4, the gluten protein emulsions treated by the individual temperatures exhibit smaller emulsion droplet particles than the control group; the heat treatment in combination with the pH12 shift treated gluten emulsion presents smaller and more uniform emulsion droplet particles.
The gluten emulsion droplet particles treated by heat treatment in combination with pH cycling exhibited smaller particle size and better uniformity than the control group, and the results were consistent with the particle size analysis. This means that the gluten proteins subjected to the heat treatment in combination with the pH cycle had better emulsification properties, and that the gluten proteins subjected to the 80℃in combination with the pH cycle had the best emulsification effect, which was consistent with the results of the above-described emulsification activity and emulsification stability experiments.
Example five
Free thiol content determination
(1) And (3) preparation of a reagent:
2.08g of Tris (hydroxymethyl) aminomethane (Tris), 1.38g of glycine and 0.24g of disodium ethylenediamine tetraacetate (EDTA) are weighed respectively, put into a 200mL volumetric flask, deionized water is used for volume fixing, and then hydrochloric acid solution is used for adjusting pH to 8.0, so that a TGE reagent (Tris-glycine-EDTA buffer solution) can be obtained. 100mL of the prepared TGE reagent was placed in a beaker, 2.5g of Sodium Dodecyl Sulfate (SDS) was added thereto, and the mixture was stirred well by using a glass rod, thereby obtaining an SDS-TGE reagent. Then 50mL of the prepared TGE reagent is taken in a beaker, 0.2g of 5,5 '-dithiobis (2-nitrobenzoic acid) (DTNB) is added into the beaker, and after the mixture is fully and uniformly stirred by using a stirring rod, the pH value is readjusted to 8.0 by using a hydrochloric acid solution, so that the Ellman's reagent can be obtained.
(2) Test procedure
Experiments were performed following modification of the method of Beveridge et al (1974). 3mL SDS-TGE buffer was pipetted into a 10mL centrifuge tube using a 5mL wide range pipette, and then 30mg protein sample was added to the centrifuge tube. After 30min of complete dissolution and vortex mixing with a vortex at 10min intervals, 30 μl of Ellman's reagent was added to the centrifuge tube for 30min of reaction, and the reaction was strictly protected from light. After the reaction, the protein solution is centrifuged for 20min at the temperature of 4 ℃ by using a refrigerated centrifuge under the centrifugal force of 8000g, and after the centrifugation is finished, the supernatant is carefully poured into a centrifuge tube wrapped with tinfoil to prevent errors of experimental results. In use, 1mL of supernatant was aspirated into a specific quartz dish, absorbance of different protein samples at 412nm was measured, and the UV spectrophotometer was calibrated with SDS-TGE solution. Three replicates were run for each sample and the final results averaged.
Mercapto content (μmol/g) =a 412 /C×73.53(2-3)
Wherein: a is that 412 : absorbance measured at 412nm, C: sample concentration (mg/mL)
As shown in FIG. 5, the 9 treatment groups all had a certain effect on the free thiol content of the gluten. Wherein the free thiol content of the gluten protein heat treated alone is increased (p < 0.05) compared with the control group, and the free thiol content is gradually increased along with the temperature rise; the free thiol content of the gluten protein was significantly increased (p < 0.05) by heat treatment in combination with pH12 shift treatment and increased with increasing temperature. The free thiol content of the gluten protein treated by the heat treatment combined with the pH cycle significantly increased (p < 0.05) compared with the control group, and the free thiol content significantly increased (p < 0.05) with the temperature. The free thiol content of the gluten protein after the treatment of the pH cycle at 40 ℃,60 ℃ and 80 ℃ is increased to 5.95 mu mol/g,14.68 mu mol/g and 15.27 mu mol/g respectively.
The results show that the control group has less free mercapto group content and a larger disulfide bond proportion. During the heat treatment, the structure of the gluten protein is changed, disulfide bonds are broken to a certain extent, so that the gluten protein is converted into free sulfhydryl groups, and the content of the free sulfhydryl groups of the protein after the heat treatment is increased. Meanwhile, in the alkaline denaturation process, the tertiary structure of the gluten protein is greatly changed, the secondary structure is also changed, the protein structure is changed to cause an exchange reaction of-SH/S-S, and the content of free sulfhydryl is greatly increased. Although the cysteine (Cys) content in gluten proteins is very low and mainly exists in the form of S-S, the peptide chain of gluten proteins is unfolded and broken after alkaline denaturation, and the interconversion between free sulfhydryl groups and disulfide bonds is also responsible for the large changes in the form of Cys present therein. Disulfide bond cleavage converts into free sulfhydryl groups, which promotes the formation of protein molecules of relatively small molecular mass, and increases the solubility of gluten proteins, thereby causing a change in emulsifying properties.
Example 6
Surface hydrophobicity determination
8-aniline-1-naphthalene sulfonic Acid (ANS) can bind to exposed hydrophobic groups of protein molecules and thus, surface hydrophobicity of differently treated gluten samples was characterized using ANS as a fluorescent probe.
First, 10mM Phosphate Buffer (PBS) with pH of 7.0 was prepared, gluten samples treated differently were diluted in PBS buffer at a concentration of 0.05-0.5mg/mL, and 5 concentration gradients were set for each protein sample treatment group. 10uL of 8.0mM ANS solution in PBS buffer was accurately pipetted into a 2mL protein sample solution, and each sample was reacted in the dark for 2min. After the reaction was completed, the excitation wavelength was set to 390nm and the emission wavelength was set to 470nm, and the fluorescence intensities of the different protein samples were measured with a fluorescence spectrophotometer. And taking the fluorescence intensity as an abscissa and the protein concentration as an ordinate to make a curve, wherein the slope of the initial stage of the obtained curve is the surface hydrophobicity index of the gluten proteins of different treatment groups. Three replicates were run for each sample and the final results averaged.
As shown in fig. 6, the 9 treatment groups all had some effect on the surface hydrophobicity of the gluten. Wherein the surface hydrophobicity of the gluten protein subjected to heat treatment alone is increased compared with the control group, and the surface hydrophobicity is gradually increased along with the temperature rise, but the surface hydrophobicity is not changed significantly; the surface hydrophobicity of the gluten protein treated by heat treatment combined with pH12 shift treatment increases significantly (p < 0.05) and increases with increasing temperature. The surface hydrophobicity of the gluten protein treated by the heat treatment combined with the pH cycle was significantly increased (p < 0.05) compared with the control group, but there was no significant change with increasing temperature. The surface hydrophobicity of the gluten protein subjected to the pH circulation treatment at 40 ℃,60 ℃ and 80 ℃ is increased by 364.82%,369.34% and 425.04%, respectively. The results show that the control group has poor surface hydrophobicity because gluten proteins are mostly macromolecular aggregates in a neutral environment and the exposed hydrophobic groups are less. During the heat treatment and alkali denaturation, the tertiary structure of the gluten protein is changed, the peptide chain is unfolded to expose more hydrophobic groups, and the charges carried by the gluten protein after the denaturation treatment cause electrostatic repulsion. Since the pH and temperature of the environment where the protein is located change to cause that more hydrophobic groups are exposed inside the protein molecules, water molecules are combined with the protein molecules, and a stable structural state is finally formed under the action of hydrophobic interaction and electrostatic interaction, the exposure of more hydrophobic groups is an important reason for influencing the solubility, the emulsifying property and other functional properties of the gluten protein.
The foregoing is merely a preferred embodiment of the application, and it should be noted that modifications and adaptations to those skilled in the art may be made without departing from the principles of the present application, which are intended to be comprehended within the scope of the application.
Claims (7)
1. A method for processing gluten protein, characterized in that the steps are as follows:
step 1, dissolving gluten protein in distilled water at 20-30 ℃ to prepare a gluten protein water system;
step 2, adopting pH circulation and heat treatment to the gluten protein water system, specifically, firstly adjusting the gluten protein water system to be alkaline by using an alkaline solution, stirring after heating treatment, and then adjusting the gluten protein water system to be neutral by using an acidic solution, and collecting the gluten protein water system after treatment;
step 3, centrifuging the collected gluten protein water system, and taking supernatant for freeze drying to obtain a gluten protein sample;
wherein the heat treatment is stirring at 40 ℃ to 80 ℃;
the pH cycle is combined with heat treatment to adjust the gluten protein water system to be alkaline, so that the pH value of the gluten protein water system is adjusted to 11-12;
the pH circulation is combined with heat treatment, and the acidic solution is utilized to adjust the gluten water system back to be neutral, so that the pH value of the gluten water system is adjusted to be 6.5-7.5.
2. The process of claim 1, wherein the concentration of the gluten protein water system is 5-50mg/mL.
3. The method according to claim 1, wherein the alkaline solution is NaOH solution or KOH solution.
4. The process according to claim 1, wherein the acidic solution is HCl solution, H 2 SO 4 A solution.
5. The method according to claim 1, wherein the centrifugation is carried out at 7000g at 20℃for 10min.
6. Use of the treatment method according to claim 1 in the field of food product treatment.
7. The use according to claim 6, wherein the food product comprises: protein beverage, edible packaging film, vegetable fat powder, ice cream and vegetable meat.
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