CN114668069B - Preparation method of soybean protein glycosylation modification products with different sugar contents - Google Patents
Preparation method of soybean protein glycosylation modification products with different sugar contents Download PDFInfo
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Classifications
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/14—Vegetable proteins
- A23J3/16—Vegetable proteins from soybean
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Biochemistry (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
The invention relates to the technical field of food processing, in particular to a preparation method of a soy protein glycosylation modification product with different sugar contents, which is prepared by catalyzing glycosylated soy protein with beta-amylase or beta-glucosidase. The invention can change the sugar content of glycosylated soybean protein on the basis of unchanged self-crosslinking degree of protein, and obtain soybean proteins with different sugar contents. The invention mainly establishes a soybean protein sugar content regulation model based on the change of the side chain glycosyl content of a glycosylation product by degrading sugar chains by saccharifying enzyme (beta-amylase and beta-glucosidase), the establishment of the regulation model is helpful for analyzing the important role of the introduced side chain glycosyl in the regulation of the functional property of the soybean protein, and the establishment of the method provides technical support for expanding the application of the glycosylation protein in the field of foods.
Description
Technical Field
The invention relates to the technical field of food processing, in particular to a preparation method of soybean protein glycosylation modified products with different sugar contents.
Background
The soybean protein (including 7S glycinin, 11S glycinin and soybean protein isolate) has high nutritive value, complete kinds of essential amino acids, and is similar to animal protein, and is a high-quality plant protein. In addition, the protein has good solubility, foamability and other functional properties, and the soybean protein has various properties such as solubility, emulsifying property, gelling property, foamability and the like, so that the soybean protein is widely applied in the food industry, for example, the soybean protein is used as an emulsifying agent to be added into the preparation of baked food, frozen food and soup food, so that the state of the product is stable; the soybean protein can be used in flour food to increase gluten strength; the soybean protein can also be used as an antibacterial fresh-keeping packaging material of foods, etc. But the solubility, foamability, etc. properties of natural soy proteins often do not meet the product requirements. Therefore, it is necessary to modify the soy protein to obtain the desired functional properties.
Maltodextrin, also known as water-soluble dextrin, is widely used in the food industry, for example, because of its good emulsifying and thickening properties, as a substitute for fat in food systems; the sugar candy can be added into the candy to reduce the risk of diabetes caused by the candy; is easy to be absorbed by human body, and is often used as a functional drink for athletes, a formula component in infant formula milk powder and the like.
Under the condition of a certain temperature and humidity, the Maillard reaction can introduce hydrophilic carbonyl groups of sugar molecules into protein molecules by changing the molecular structure of the protein, and the Maillard reaction has high safety without adding chemical reagents. The functional properties of soy proteins can be significantly improved by the maillard reaction. Currently, protein glycosylation modification based on the maillard pathway generally employs two ways to regulate the amount of protein glycosyl introduced: one approach is to control the glycosylation reaction time, but this method has certain limitations, such as the presence of excessive reactions that produce melanoids and other harmful substances (MAILLARD L C, 1912), and will destroy the functional properties of the protein; alternatively, proteins having different amounts of introduced sugar groups can be obtained by changing the molecular weight of the introduced sugar groups, such as introducing monosaccharides, oligosaccharides, and polysaccharides, respectively, into the protein. It is noted that the Maillard reaction is accompanied by self-crosslinking of the protein (Oliveira F C, coimbra J S R, oliveira E B, etc., 2016) at the same time as the introduction of the glycosyl groups. Thus, the above method makes it difficult to define the potential influence of protein self-crosslinking when analyzing the rule of influence of the amount of glycosyl transfer on the functional properties of Maillard products.
By utilizing highly specific glycosidases (such as beta-amylase and beta-glucosidase) to break the oligosaccharide chains to different degrees, different sugar chain length regulation modes (1 maltose unit or 1 glucose unit is shortened) can be implemented, so that the sugar content of glycosylated soybean protein is regulated, soybean protein glycosylation products with different sugar contents are obtained, and the structure-activity relationship of Maillard products is analyzed by taking the soybean protein glycosylation products as a model, so that the soybean protein glycosylation products have remarkable advantages.
Disclosure of Invention
The invention aims to provide a method for regulating and controlling the functional property of soybean protein by directionally breaking Maillard co-glycan chains, which aims to solve the problems in the prior art, and is mainly used for analyzing the influence of the change of sugar molecular content on the functional property of the soybean protein on the basis of keeping the self-crosslinking degree of the protein unchanged when protein glycosylation is realized by Maillard glycosylation reaction. And obtaining a soy protein glycosylation product by adopting Maillard reaction, then changing the side chain glycosyl content of the glycosylation product based on hydrolysis (beta-amylase and beta-glucosidase), obtaining soy isolated proteins with different sugar contents, and establishing a soy protein sugar content regulation model. The soybean protein glycosylation modification is realized by using amino-rich soybean protein and carbonyl-rich maltodextrin or resistant dextrin as substrates to generate Maillard reaction. On the basis of unchanged self-crosslinking degree of the protein, the sugar content of the glycosylated soybean protein is changed, and the soybean proteins with different sugar contents are obtained. The establishment of the soybean protein sugar content regulation model is helpful for analyzing the important role of side chain glycosyl in the functional property of soybean protein, the establishment of the method provides technical support for expanding the application of the protein in the field of foods, and the invention provides the following scheme for realizing the purposes:
A process for preparing the glycosylation modified products of soybean protein with different sugar contents includes such steps as preparing the glycosylated soybean protein under the catalysis of beta-amylase or beta-glucosidase.
Preferably, the soybean protein glycosylation modification product is prepared from soybean protein and maltodextrin through Maillard reaction.
The preparation method further comprises the steps of enzyme deactivation, dialysis and drying, so that glycosylation modified products which do not change the main chain of the soybean protein molecule and only change the sugar content can be obtained, and the soybean protein sugar content regulation model is established.
By utilizing the method provided by the invention, the Maillard co-glycan chain can be directionally broken, so that the purpose of regulating and controlling the functional property of the soybean protein is achieved.
Preferably, the preparation method of the soy protein glycosylation modification products with different sugar contents comprises the steps of adding glycosidase (beta-amylase and beta-glucosidase) into the glycosylation soy protein dispersion liquid at 50-55 ℃ and vibrating at constant temperature for 5-80 min. And after the reaction is finished, inactivating enzyme, dialyzing to remove free sugar molecules, and freeze-drying to obtain the glycosylation modification products with different sugar contents.
In the present invention, the beta-amylase has an optimum pH in the range of 4.0 to 7.0, an optimum catalytic temperature of 50℃and is deactivated when the temperature reaches 70 ℃. The optimal pH value range of the beta-glucosidase is 5.0-7.0, the optimal catalysis temperature is 40-60 ℃, and the beta-glucosidase is deactivated when the temperature reaches 70 ℃. In the invention, the maltodextrin which is covalently crosslinked into the soybean protein by beta-amylase or beta-glucosidase is broken by utilizing a highly specific enzymatic reaction, the sugar chains can be cut off to different degrees by controlling the hydrolysis reaction time, and the structure and the functional properties of the products with different sugar content modification are changed compared with those of the glycosylated products, so that the glycosylated soybean protein with different functional properties can be obtained.
Further, the conditions for inactivating the enzyme are as follows: and after the reaction is finished, immediately taking out, putting the mixture into a water bath kettle with the temperature of 85-95 ℃ to inactivate enzymes for 5-10 min, and then cooling the mixture to room temperature.
The function of enzyme deactivation is to terminate the hydrolysis reaction and deactivate the enzyme.
In a preferred embodiment, the present invention provides a process for the preparation of soy protein glycosylation products having different sugar content, comprising the steps of:
Taking soybean protein and maltodextrin as raw materials, preparing soybean protein dispersion liquid, preparing maltodextrin solution, carrying out Maillard reaction on the soybean protein and the maltodextrin under a damp-heat condition, carrying out acid precipitation, centrifugally collecting precipitate, regulating pH, dialyzing and drying to obtain glycosylated soybean protein; and then, under the catalysis of beta-amylase or beta-glucosidase, glycosylation modified products with different sugar contents are obtained, and finally, the soy protein glycosylation products with different sugar contents are obtained through enzyme deactivation, dialysis and drying.
Preferably, the soy protein is selected from the group consisting of 7S glycinin, 11S glycinin, soy protein isolate; preferably, the soy protein is a soy protein dispersion, and the dispersion is prepared under the following conditions: the soybean protein is taken as a raw material, a certain volume of distilled water is added to prepare soybean protein dispersion liquid, then the soybean protein dispersion liquid is heated in a water bath at 90-100 ℃ for 10min, and then cooled to 37 ℃, the pH value is regulated to 7.5-8.5, and preferably, the pH value is regulated to 8.
The soybean protein has high nutritive value, complete kinds of essential amino acids, and is similar to animal protein, and is one kind of high quality plant protein. Soy proteins are widely used in many food industry applications for their good nutritional quality and various functional properties. The portion of soy protein precipitated between pH4.5 and 4.8 according to high-speed centrifugation is called glycinin, and heat treatment can stretch the glycinin, which is beneficial to promote Maillard reaction.
Preferably, the maltodextrin is maltodextrin solution, and the preparation conditions of the solution are as follows: maltodextrin is used as raw material, a certain volume of distilled water is added to prepare maltodextrin solution, the pH value is adjusted to 7.5-8.5, and preferably, the pH value is adjusted to 8.
Maltodextrin has the characteristics of low sweetness, no peculiar smell, easy digestion, good solubility, strong thickening property, good carrier property and good stability, is difficult to deteriorate, is widely applied to various foods, and in recent years, besides being used as a filling agent and a thickening agent of foods, the maltodextrin can also be used as a drying aid and an embedding wall material to improve the function of protein, so that the application scene of the maltodextrin is further expanded. Maltodextrin contains abundant hydrophilic carbonyl groups, can perform Maillard reaction, and can obviously improve the solubility and emulsifying property of the whole molecule. The maltodextrin is fully dissolved in distilled water, which is more favorable for Maillard reaction.
Preferably, the preparation method of the soybean protein glycosylation product comprises the following steps: mixing the soybean protein dispersion liquid and the maltodextrin solution according to the mass ratio of 3:1-1:3, enabling the concentration of the final solution to be 2% -6%, stirring and heating for 20-120 min at the temperature of 85-95 ℃ to obtain a soybean protein-maltodextrin mixed solution, removing free sugar molecules from the solution through an alkali-dissolution acid precipitation and dialysis method, and freeze-drying the product to prepare the glycosylated soybean protein.
Preferably, the soybean protein dispersion liquid and the maltodextrin solution are mixed according to a mass ratio of 1:2, so that the final solution concentration is 4%, and the mixture is stirred and heated for 20min at a temperature of 95 ℃ to obtain the soybean protein-maltodextrin mixed solution.
Under the condition of a certain temperature and humidity, the Maillard reaction can introduce hydrophilic carbonyl groups of sugar molecules into protein molecules by changing the molecular structure of the protein, change the molecular volume, charge and amino acid composition, further improve the structural and functional properties of the protein and improve the processing characteristics of the protein. Compared with original protein, the secondary structure of the glycosylation product is changed, and the foamability, foam stability, emulsifying property and emulsifying stability are obviously improved, so that a theoretical basis is provided for producing functional ingredients of plant protein. Therefore, there is a wide prospect of improving the structural and functional properties of proteins by effecting glycosylation reactions between protein molecules and sugar molecules through Maillard reactions.
Preferably, the alkali-soluble acid precipitation conditions are as follows: the pH value of the protein-sugar solution is regulated to 4.5, the centrifugation is carried out for 5 to 15min at 3000 to 5000r/min, the sediment is collected, distilled water is added for dissolution, and the pH value is regulated to 7.0.
In the present invention, precipitation of the soy protein-maltodextrin solution occurs at ph=4.5, soy protein is precipitated, unreacted maltodextrin is in the supernatant, and the precipitate is then redissolved in distilled water to obtain a protein dispersion. The method can effectively remove the maltodextrin molecules which do not participate in the reaction, and is beneficial to the subsequent reaction.
Further, the dialysis conditions are that the solution is subjected to dialysis (8-14 kDa) at 4℃for 24 to 48 hours, preferably, the dialysis time is 24 hours.
The dialysis is completed by adopting an 8-14kDa dialysis bag, filling a sample solution into the bag, immersing the dialysis bag into water or buffer solution, trapping soybean protein with large molecular weight in the sample solution in the bag, and separating salt and maltodextrin molecules (less than or equal to 5 kDa) out of the bag until the concentration of the inner side and the outer side of the bag reach balance. The method effectively removes salt molecules and free maltodextrin molecules in the dispersion liquid, and purifies soybean protein glycosylation products.
Meanwhile, the invention also provides a soybean protein glycosylation modification product with different sugar contents, which is prepared by the method.
Finally, the invention also provides a soybean protein sugar content regulation model established by the directional fracture of the oligosaccharide chain, which is characterized by providing theoretical support for elucidating important roles of protein side chain glycosyl in protein functional properties.
Based on Maillard reaction principle, soybean protein rich in free amino and maltodextrin rich in hydrophilic carbonyl are used as substrates, and crosslinking between protein molecules and sugar molecules occurs, so that soybean protein glycosylation modification is realized. The cross-linking of the soybean protein and maltodextrin enhances the functional properties of the soybean protein, such as solubility, emulsifying activity, foamability, foam stability, water retention and oil retention, apparent viscosity and viscoelasticity, so that the Maillard reaction can prepare a food ingredient with ideal functional characteristics, and the soybean protein glycosylation product can be used as a functional ingredient in foods, such as enhanced cake foaming and special population foods. The maltodextrin which is covalently crosslinked into the soy protein is broken by beta-glucosidase or beta-amylase by utilizing a high-specificity hydrolysis reaction, and sugar chains can be cut off to different degrees by controlling the hydrolysis reaction time, so that the guarantee is provided for the research on the functional property characterization of the glycosylated soy protein with different sugar contents; in addition, maillard glycosylation can produce food ingredients with desirable functional properties, and soy protein glycosylation modification products can be used as functional ingredients in foods, such as to enhance foaming of cakes and in foods for special people.
The invention discloses the following technical effects:
Based on Maillard reaction principle, maltodextrin rich in hydrophilic hydroxyl is added into soybean protein dispersion liquid rich in free amino groups so as to crosslink soybean protein fully with maltodextrin, thereby changing the characteristics of relative molecular mass, amino acid composition, molecular volume, charge and the like of the soybean protein, and even the structure of the soybean protein. Then, beta-glucosidase or beta-amylase is used for carrying out high-specificity hydrolysis reaction, and the maltodextrin which is covalently crosslinked into the soybean protein is broken, so that sugar chains are cut off to different degrees by controlling the hydrolysis reaction time, and the soybean protein isolate with different sugar contents is obtained, so that the sugar content of the glycosylated soybean protein is changed on the basis of unchanged self-crosslinking degree of the protein, the soybean protein with different sugar contents is obtained, a soybean protein sugar content regulation model is established, and then, the property change of a modified product is evaluated and characterized by a system, so that the purpose of clarifying the change rule of the soybean protein with different sugar contents in the functional property is achieved, thereby providing theoretical support for the important function of protein side chain glycosyl in the functional property of the protein, expanding the range of the protein as a functional ingredient of food, and meeting the special requirements of the protein in food processing.
Drawings
In order to more clearly illustrate the embodiments of the present invention or the technical solutions in the prior art, the drawings that are needed in the embodiments will be briefly described below, and it is obvious that the drawings in the following description are only some embodiments of the present invention, and other drawings may be obtained according to these drawings without inventive effort for a person skilled in the art.
FIG. 1 shows the grafting degree of modified SPIs with sample numbers 2, 3, 1,4 and 5 under different conditions.
FIG. 2 shows the grafting degree of modified SPIs with sample numbers 9, 8, 6, 1 and 7 under different conditions.
FIG. 3 shows the grafting degree of modified SPI of sample numbers 10, 9, 1, 11, 12 under different conditions.
Fig. 4 is a bar graph of the foamability and foam stability of samples 10, 14-16.
FIG. 5 is a graph of the fluorescence spectra of samples 10, 14-16.
Fig. 6 is a graph of commercial Soy Protein (SPI), sample 10, 14-16 apparent viscosity.
Fig. 7 is a bar graph of the foamability and foam stability of samples 10, 17-19.
FIG. 8 is a graph of the fluorescence spectra of samples 10, 17-19.
Fig. 9 is a graph of the commercial Soy Protein (SPI), sample 10, 17-19 apparent viscosity.
Detailed Description
Various exemplary embodiments of the invention will now be described in detail, which should not be considered as limiting the invention, but rather as more detailed descriptions of certain aspects, features and embodiments of the invention.
It is to be understood that the terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting of the invention. In addition, for numerical ranges in this disclosure, it is understood that each intermediate value between the upper and lower limits of the ranges is also specifically disclosed. Every smaller range between any stated value or stated range, and any other stated value or intermediate value within the stated range, is also encompassed within the invention. The upper and lower limits of these smaller ranges may independently be included or excluded in the range.
Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. Although only preferred methods and materials are described herein, any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention. All documents mentioned in this specification are incorporated by reference for the purpose of disclosing and describing the methods and/or materials associated with the documents. In case of conflict with any incorporated document, the present specification will control.
It will be apparent to those skilled in the art that various modifications and variations can be made in the specific embodiments of the invention described herein without departing from the scope or spirit of the invention. Other embodiments will be apparent to those skilled in the art from consideration of the specification of the present invention. The specification and examples of the present invention are exemplary only.
As used herein, the terms "comprising," "including," "having," "containing," and the like are intended to be inclusive and mean an inclusion, but not limited to.
Example 1
A method for regulating the functional properties of soybean protein by directionally breaking maillard co-glycan chains, comprising the following steps:
(1) The preparation conditions of the soy protein dispersion are as follows: taking soybean protein as a raw material, adding a certain volume of distilled water to prepare protein dispersion liquid, heating SPI (soy protein isolate) dispersion liquid in a water bath at 95 ℃ for 10min, cooling to 37 ℃, and regulating the pH value to 8.
(2) The preparation conditions of the maltodextrin solution are as follows: maltodextrin is used as a raw material, a certain volume of distilled water is added to prepare a maltodextrin solution, and the pH value is adjusted to 8.
(3) The preparation conditions of the soy protein glycosylation product are: mixing the soybean protein dispersion liquid and maltodextrin solution according to the mass ratio of 1:2, enabling the concentration of the final solution to be 4%, stirring and heating for 40min at the temperature of 95 ℃ to obtain a soybean protein-maltodextrin mixed solution, removing free sugar molecules from the solution through alkali dissolution, acid precipitation and dialysis, and freeze-drying the product to prepare the glycosylated soybean protein.
(4) The alkali dissolution and acid precipitation conditions are as follows: regulating the pH value of the soybean protein-maltodextrin solution to 4.5, centrifuging for 10min at 3000r/min, collecting precipitate, adding distilled water for dissolving, and regulating the pH value to 7.0.
(5) The dialysis conditions were that the solution was subjected to dialysis (8-14 kDa) at 4℃for 24 hours.
Example 2
The difference from example 1 was only that the final concentration of the reaction solution in step (3) was changed to 2%.
Example 3
The difference from example 1 was only that the final concentration of the reaction solution in step (3) was changed to 3%.
Example 4
The difference from example 1 was only that the final concentration of the reaction solution in step (3) was changed to 5%.
Example 5
The difference from example 1 was only that the final concentration of the reaction solution in step (3) was changed to 6%.
Example 6
The only difference from example 1 is that the mass ratio of the soy protein dispersion of step (3) and the maltodextrin solution was changed to 1:1.
Example 7
The only difference from example 1 is that the mass ratio of the soy protein dispersion of step (3) and the maltodextrin solution was changed to 1:3.
Example 8
The only difference from example 1 is that the mass ratio of the soy protein dispersion of step (3) and the maltodextrin solution was changed to 2:1.
Example 9-1
The only difference from example 1 is that the mass ratio of the soy protein dispersion and maltodextrin solution of step (3) was changed to 3:1.
Example 9-2
The difference from example 1 was only that the reaction time of step (3) was changed to 30min.
Example 10
The difference from example 1 was only that the reaction time of step (3) was changed to 20min.
Example 11
The only difference from example 1 is that the reaction time of step (3) was changed to 60min.
Example 12
The difference from example 1 was only that the reaction time of step (3) was changed to 120min.
Example 13
The only difference from example 1 is that the maltodextrin of step (2) is replaced with a resistant dextrin.
Experimental example 1
The determination of free amino groups was performed on examples 1-12 (labeled as samples 1-12), and the content of free amino groups was compared to determine the optimum condition for Maillard reaction; the specific process is as follows:
1.1 determination of free amino groups
The free amino group is the content of free amino groups contained in the protein molecule, and the Maillard reaction can utilize the free amino groups of the protein to react with sugar molecules to convert the free amino groups into a combined state, so that the content of the free amino groups is reduced.
The grafting Degree (DG) of the glycosylation product was calculated as follows:
( C 0 is the free amino content before reaction; c 1 is the free amino content after the reaction )
The results are shown in FIGS. 1 to 3.
Example 14
A method for regulating the functional properties of a soy protein by directionally cleaving a oligosaccharide chain, comprising the steps of:
(1) The Maillard reaction conditions determined in experimental example 1 were used to prepare a glycosylated product, beta-amylase was added at 50℃in an amount of 150U/g protein, and the mixture was shaken at constant temperature for 5min. After the reaction is finished, inactivating enzyme, freeze-drying to obtain a modified product, dialyzing to remove free maltodextrin, and freeze-drying the glycosylation modified product for later use.
(2) Enzyme deactivation: after the reaction is finished, taking out the sample, putting the sample into a water bath kettle at 90 ℃ to inactivate enzyme for 5 minutes, and cooling the sample to room temperature.
Example 15
The difference from example 14 was only that the reaction time of step (1) was changed to 40min.
Example 16
The difference from example 14 was only that the reaction time of step (1) was changed to 80min.
Example 17
A method for regulating the functional properties of a soy protein by directionally cleaving a oligosaccharide chain, comprising the steps of:
(1) The Maillard reaction conditions determined in experimental example 1 were used to prepare a glycosylated product, beta-glucosidase was added at 50℃in an amount of 90U/g protein, and the mixture was shaken at constant temperature for 5min. After the reaction is finished, inactivating enzyme, freeze-drying to obtain a modified product, dialyzing to remove free maltodextrin, and freeze-drying the glycosylation modified product for later use.
(2) Enzyme deactivation: after the reaction is finished, taking out the sample, putting the sample into a water bath kettle at 90 ℃ to inactivate enzyme for 5 minutes, and cooling the sample to room temperature.
Example 18
The difference from example 17 was only that the reaction time of step (1) was changed to 20min.
Example 19
The difference from example 17 was only that the reaction time of step (1) was changed to 80min.
Example 20
A method for regulating the functional properties of a soy protein by directionally cleaving a oligosaccharide chain, comprising the steps of:
(1) The Maillard reaction conditions determined in experimental example 1 were used to prepare a glycosylated product, beta-amylase was added at 50℃in an amount of 90U/g protein, and the mixture was shaken at constant temperature for 5min. After the reaction is finished, inactivating enzyme, freeze-drying to obtain a modified product, dialyzing to remove free resistant dextrin, and freeze-drying the glycosylation modified product for later use.
(2) Enzyme deactivation: after the reaction is finished, taking out the sample, putting the sample into a water bath kettle at 90 ℃ to inactivate enzyme for 5 minutes, and cooling the sample to room temperature.
Example 21
The difference from example 20 was only that the reaction time of step (1) was changed to 40min.
Example 22
The difference from example 20 was only that the reaction time of step (1) was changed to 80min.
Experimental example 2
Performance verification experiments, comparative technical effects were performed on examples 14-16 (labeled as samples 14-16), sample 10 and the unmodified soy protein purchased in the market; the sugar content experiments were performed on examples 20-22 (labeled as samples 20-22) and on example 13 (labeled as sample 13) with the following results:
2.1 determination of sugar content in glycosylation modification products
Colorimetry (colorimetry) is a method of determining the content of a component to be measured by comparing or measuring the color depth of a solution of a colored substance. The principle of determining the sugar content in the glycosylation modification product by using a colorimetric method is that polysaccharide is firstly hydrolyzed into monosaccharide under the action of sulfuric acid, and is rapidly dehydrated to generate a furfural derivative, and finally the furfural derivative and phenol are used for generating an orange-yellow compound, and the sugar content in the solution can be determined according to the absorption intensity of light by a colored solution.
Drawing a glucose standard curve: preparing 0.1mg/mL glucose standard solution, respectively taking 0, 0.2, 0.4, 0.6, 0.8 and 1.0mL glucose standard solution into a test tube with a plug, supplementing 1.0mL glucose standard solution with distilled water, respectively adding 1.0mL phenol solution with 5% concentration, rapidly adding 5.0mL concentrated sulfuric acid, shaking uniformly, and standing for 10min. Then treated in a water bath at 30℃for 20min. The absorbance of the reaction solution was measured at 490 nm. The abscissa of the standard curve is the glucose mass concentration, and the ordinate is the absorbance.
Determination of the samples: the sample (4%, w/v) was diluted 100-fold, and 1mL of the sample solution was used to measure the absorbance of the sample in the same manner, and the results are shown in tables 1 and 2.
TABLE 1 sugar content (maltodextrin)
TABLE 2 sugar content (resistant dextrin)
2.2 Foamability and foam stability
Foam generally refers to a dispersion of gas bubbles dispersed in a continuous liquid or semi-solid phase containing a surfactant. Protein foam characteristics include foam-forming ability, which refers to the amount of foam produced under certain conditions (e.g., whipping), and foam-stabilizing ability, which refers to the stability (over time) of the foam formed.
The calculation method comprises the following steps:
Protein samples were dissolved in phosphate buffer (pH 7.0) to prepare a protein solution with a mass concentration of 10 g/L. 100mL of this solution was whipped at 12000r/min for 1min, data recorded, and measured in parallel for 3 times [11]. The formulas for protein foamability (F C) and foam stability (F S) are formula (2) and formula (3), respectively
Wherein: v L is the volume of liquid before whipping; v 0 is the volume of foam immediately after whipping has ceased; v 30 is the volume of foam at 30min after whipping and the results are shown in FIG. 4.
2.3 Solubility
The solubility of a substance in various solvents is often expressed in terms of solubility. Solubility is one of the main functional properties of proteins, and more importantly, solubility is the premise and basis for physiological and other processing functions of proteins. The measurement method is as follows: protein samples were dissolved in a buffer at pH 7.0 to prepare a 2g/L protein solution. After vortexing, storage at 4 ℃ was carried out to allow for adequate hydration. Centrifuging for 20min at 8000r/min the next day, collecting supernatant, and measuring the content of soluble protein with Fu Lin Fenfa. Protein solubility is expressed as the ratio of soluble protein content in the sample to be tested, and the results are shown in Table 3.
TABLE 3 solubility
2.4 Hydrated particle size distribution and Zeta potential
The hydrated particle size reflects the aggregation behavior of the glycosylation modification product. Zeta potential is the potential of the shear plane of charged particles in a protein solution, and is typically used to measure the attractive and repulsive forces between particles; is also an important parameter for measuring the dispersion stability of a colloid system.
A protein dispersion of a certain concentration was prepared and the concentration was diluted to 0.1mg/mL (pH 7.0), filtered with a 0.45 μm water film, and then the hydrated particle size distribution and Zeta potential of the sample were measured 3 times in parallel with a particle size analyzer, and the results are shown in Table 4.
TABLE 4 particle size distribution by hydration and zeta potential
2.5 In-fluorescence Spectrometry
The fluorescent effect is generated by fluorescent substances in the sample, which can be derived from the inside of the food sample, i.e. by the components of the sample itself, called endogenous fluorescent substances.
A protein sample is dissolved in 0.01mol/L phosphate buffer solution (pH 7.0) to prepare 1mg/mL protein sample solution, and then the solution is centrifuged for 15min under 10000r/min, 4mL of supernatant is taken, and the emission spectrum in the range of 300-400 nm is scanned under the conditions that the emission wavelength is 290nm and the excitation and emission slit luminosity is 5 nm. The results are plotted in FIG. 5, with wavelength on the abscissa and relative fluorescence intensity on the ordinate.
2.6 Determination of apparent viscosity
Apparent viscosity refers to the ratio of the corresponding shear stress to the shear rate at a certain velocity gradient. The apparent viscosity value can reflect the fluidity of the subject to some extent.
The apparent viscosity of the protein was measured with a Markov rheometer. A protein sample solution (pH 7.0) was prepared at a mass concentration of 4% (w/v). For measurement, the sample dispersion was slowly poured into a full-charged jig (conical plate with a diameter of 60mm and a cone angle of 0.5 °). The apparent viscosity of the test sample was measured at a temperature of 25℃and a frequency of 0.1 to 100s -1, and the result is shown in FIG. 6.
Experimental example 3
Performance verification experiments were performed on examples 17-19 (labeled as samples 17-19), sample 10 and the unmodified soy protein purchased in the market, comparing the technical effects, as follows:
3.1 determination of sugar content in glycosylation modification products
The results are shown in Table 5.
TABLE 5 sugar content
3.2 Foamability and foam stability
Foam generally refers to a dispersion of gas bubbles dispersed in a continuous liquid or semi-solid phase containing a surfactant. Protein foam characteristics include foam-forming ability, which refers to the amount of foam produced under certain conditions (e.g., whipping), and foam-stabilizing ability, which refers to the stability (over time) of the foam formed.
The calculation method comprises the following steps:
protein samples were dissolved in phosphate buffer (pH 7.5) to prepare a protein solution with a mass concentration of 10 g/L. 100mL of this solution was whipped at 12000r/min for 1min, data recorded, and measured in parallel for 3 times [11]. The formulas for protein foamability (F C) and foam stability (F S) are formula (2) and formula (3), respectively
Wherein: v L is the volume of liquid before whipping; v 0 is the volume of foam immediately after whipping has ceased; v 30 is the volume of foam at 30min after whipping and the results are shown in FIG. 7.
3.3 Solubility
The results are shown in Table 6.
TABLE 6 solubility
3.4 Hydrated particle size distribution and Zeta potential
The hydrated particle size reflects the aggregation behavior of the glycosylation modification product. Zeta potential is the potential of the shear plane of charged particles in a protein solution, and is typically used to measure the attractive and repulsive forces between particles; is also an important parameter for measuring the dispersion stability of a colloid system.
A protein dispersion was prepared at a concentration and diluted to 0.1mg/mL (pH 7.5), filtered with a 0.45 μm water film, and the hydrated particle size distribution and Zeta potential of the sample were measured 3 times in parallel with a particle size analyzer, and the results are shown in Table 7.
TABLE 7 particle size distribution by hydration and zeta potential
3.5 In-fluorescence Spectrometry
The fluorescent effect is generated by fluorescent substances in the sample, which can be derived from the inside of the food sample, i.e. by the components of the sample itself, called endogenous fluorescent substances.
A protein sample is dissolved in 0.01mol/L phosphate buffer solution (pH 7.5) to prepare 1mg/mL protein sample solution, and then the solution is centrifuged for 15min under 10000r/min, 4mL of supernatant is taken, and the emission spectrum in the range of 300-400 nm is scanned under the conditions that the emission wavelength is 290nm and the excitation and emission slit luminosity is 5 nm. The results are plotted in FIG. 8, with wavelength on the abscissa and relative fluorescence intensity on the ordinate.
3.6 Determination of apparent viscosity
The apparent viscosity of the protein was measured with a Markov rheometer. A protein sample solution (pH 7.5) was prepared at a mass concentration of 4% (w/v). For measurement, the sample dispersion was slowly poured into a full-charged jig (conical plate with a diameter of 60mm and a cone angle of 0.5 °). The apparent viscosity of the test sample was measured at a temperature of 25℃and a frequency of 0.1 to 100s-1, and the result is shown in FIG. 9.
Claims (12)
1. A method for preparing soy protein glycosylation modification products having different sugar content, the method comprising the steps of:
Taking soybean protein and maltodextrin as raw materials, preparing soybean protein dispersion liquid, preparing maltodextrin solution, carrying out Maillard reaction on the soybean protein and the maltodextrin under a damp-heat condition, carrying out acid precipitation, centrifugally collecting precipitate, regulating pH, dialyzing and drying to obtain glycosylated soybean protein; and then, utilizing beta-amylase or beta-glucosidase to obtain glycosylation modification products with different sugar contents, specifically comprising enzymolysis, enzyme deactivation, dialysis and drying to obtain the glycosylation modification products without changing the main chain of the soybean protein molecule and only changing the sugar content, and establishing the soybean protein sugar content regulation model.
2. The method of claim 1, wherein the soy protein is selected from the group consisting of 7S glycinin, 11S glycinin, and soy protein isolate; the soybean protein is in the form of soybean protein dispersion liquid, beta-amylase is added into the soybean protein dispersion liquid at 50-55 ℃ or beta-glucosidase is added into the soybean protein dispersion liquid at 50-55 ℃, the adding amount is 50-150U/g protein, the soybean protein is subjected to constant temperature oscillation for 5-80 min, after the reaction is finished, enzyme is inactivated, free sugar molecules are removed by dialysis, and the soybean protein is subjected to freeze drying, so that the glycosylation modified products with different sugar contents are obtained.
3. The preparation method according to claim 2, wherein the pH value is in the range of 4.0 to 7.0 when beta-amylase is used as a catalyst; when beta-glucosidase is used as a catalyst, the pH value range is 5.0-7.0.
4. The method of claim 1, wherein the conditions for the step of inactivating enzyme are: and after the reaction is finished, immediately taking out, putting the mixture into a water bath kettle with the temperature of 85-95 ℃ to inactivate enzymes for 5-10 min, and then cooling the mixture to room temperature.
5. The method of claim 1, wherein the soy protein dispersion is formulated under the following conditions: taking soybean protein as a raw material, adding a certain volume of distilled water to prepare soybean protein dispersion liquid, heating the soybean protein dispersion liquid in a water bath at 90-100 ℃ for 10min, cooling to 37 ℃, and regulating the pH value to 7.5-8.5.
6. The preparation method according to claim 1, wherein the maltodextrin solution is formulated under the following conditions: maltodextrin is used as raw material, a certain volume of distilled water is added to prepare maltodextrin solution, and the pH value is regulated to 7.5-8.5.
7. The method according to claim 1, wherein the maillard reaction conditions are: mixing the soybean protein dispersion liquid and the maltodextrin solution according to the mass ratio of 3:1-1:3, enabling the concentration of the final solution to be 2% -6%, and stirring and heating the mixture at the temperature of 85-95 ℃ for reacting for 20-120 min to obtain different soybean protein-maltodextrin mixed solutions.
8. The method according to claim 1, wherein the acid precipitation conditions are: the pH of the soy protein-maltodextrin solution was adjusted to 4.5.
9. The method according to claim 1, wherein the centrifugation conditions are 3000 to 5000r/min for 5 to 15min.
10. The method according to claim 1, wherein the pH-adjusting condition is dissolution with distilled water and adjustment of pH to 7.0.
11. The method according to claim 1, wherein the dialysis conditions are that the solution is subjected to dialysis (8-14 kDa) at 4℃for 24-48 hours; the material in the dialysis bag is collected as a solution from which free sugar molecules are removed, and dried to give a glycosylated soy protein.
12. A soy protein glycosylation modification product with different sugar content prepared according to any one of claims 1-11.
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Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103931874A (en) * | 2014-05-07 | 2014-07-23 | 河南工业大学 | Method for preparing low-sensitivity soybean protein powder by combination of glycosylation and enzymatic modification |
| CN104286370A (en) * | 2014-08-20 | 2015-01-21 | 华南理工大学 | Method for preparing functional soybean protein by enzyme-assistant subcritical water method |
| CN115336667A (en) * | 2022-08-25 | 2022-11-15 | 齐齐哈尔大学 | Soybean protein modified product and preparation method thereof |
| CN116391788A (en) * | 2023-04-13 | 2023-07-07 | 东北农业大学 | Method for preparing high-foamability soybean protein powder by Maillard-assisted enzymolysis |
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| CN101797024B (en) * | 2010-03-26 | 2012-09-05 | 东莞徐记食品有限公司 | Preparation method and application of antioxidant syrup |
| CN103652316A (en) * | 2013-12-18 | 2014-03-26 | 东北农业大学 | Preparation method of modified isolated soy protein with high emulsibility and high solubility |
| CN103976052B (en) * | 2014-05-07 | 2016-06-22 | 中华全国供销合作总社杭州茶叶研究所 | A kind of fermented type tea juice and preparation method thereof |
| CN106148462A (en) * | 2016-07-19 | 2016-11-23 | 齐齐哈尔大学 | Semen sojae atricolor glycopeptide with bioactive functions and preparation method thereof |
| CN106480137B (en) * | 2016-11-17 | 2019-10-29 | 武汉轻工大学 | A kind of endogenous sugar improves the method and products thereof of rice residue protein functional characteristic |
| CN109730190A (en) * | 2019-02-22 | 2019-05-10 | 黑龙江冰泉多多保健食品有限责任公司 | A kind of high emulsibility soybean protein powder producing method |
| CN114317660B (en) * | 2022-01-29 | 2023-10-27 | 云南农业大学 | Method for improving utilization rate of walnut meal protein |
-
2022
- 2022-04-25 CN CN202210438352.XA patent/CN114668069B/en active Active
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103931874A (en) * | 2014-05-07 | 2014-07-23 | 河南工业大学 | Method for preparing low-sensitivity soybean protein powder by combination of glycosylation and enzymatic modification |
| CN104286370A (en) * | 2014-08-20 | 2015-01-21 | 华南理工大学 | Method for preparing functional soybean protein by enzyme-assistant subcritical water method |
| CN115336667A (en) * | 2022-08-25 | 2022-11-15 | 齐齐哈尔大学 | Soybean protein modified product and preparation method thereof |
| CN116391788A (en) * | 2023-04-13 | 2023-07-07 | 东北农业大学 | Method for preparing high-foamability soybean protein powder by Maillard-assisted enzymolysis |
Non-Patent Citations (1)
| Title |
|---|
| 糖含量对大豆蛋白起泡性的影响;薛远等;中国食品学报;20231031;第23卷(第10期);第118-124页 * |
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