CN112914105B - Method for improving emulsibility of yeast soluble beta-glucan - Google Patents
Method for improving emulsibility of yeast soluble beta-glucan Download PDFInfo
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- 229920002498 Beta-glucan Polymers 0.000 title claims abstract description 77
- FYGDTMLNYKFZSV-URKRLVJHSA-N (2s,3r,4s,5s,6r)-2-[(2r,4r,5r,6s)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2r,4r,5r,6s)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1[C@@H](CO)O[C@@H](OC2[C@H](O[C@H](O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-URKRLVJHSA-N 0.000 title claims abstract description 74
- 240000004808 Saccharomyces cerevisiae Species 0.000 title claims abstract description 65
- 238000000034 method Methods 0.000 title claims abstract description 21
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims abstract description 38
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 34
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 34
- 235000017060 Arachis glabrata Nutrition 0.000 claims abstract description 19
- 244000105624 Arachis hypogaea Species 0.000 claims abstract description 19
- 235000010777 Arachis hypogaea Nutrition 0.000 claims abstract description 19
- 235000018262 Arachis monticola Nutrition 0.000 claims abstract description 19
- 238000006243 chemical reaction Methods 0.000 claims abstract description 19
- 235000020232 peanut Nutrition 0.000 claims abstract description 19
- 238000010438 heat treatment Methods 0.000 claims abstract description 12
- 239000008367 deionised water Substances 0.000 claims abstract description 11
- 229910021641 deionized water Inorganic materials 0.000 claims abstract description 11
- 238000003756 stirring Methods 0.000 claims abstract description 11
- 239000007853 buffer solution Substances 0.000 claims abstract description 10
- 230000000887 hydrating effect Effects 0.000 claims abstract description 10
- 238000002156 mixing Methods 0.000 claims abstract description 10
- 150000001875 compounds Chemical class 0.000 claims abstract description 8
- 239000011259 mixed solution Substances 0.000 claims abstract description 6
- 238000005119 centrifugation Methods 0.000 claims abstract description 3
- 238000004108 freeze drying Methods 0.000 claims abstract description 3
- 239000000725 suspension Substances 0.000 claims description 24
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 12
- 108090000790 Enzymes Proteins 0.000 claims description 8
- 102000004190 Enzymes Human genes 0.000 claims description 8
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 8
- 238000009835 boiling Methods 0.000 claims description 8
- 230000007062 hydrolysis Effects 0.000 claims description 8
- 238000006460 hydrolysis reaction Methods 0.000 claims description 8
- 230000000415 inactivating effect Effects 0.000 claims description 8
- 239000006228 supernatant Substances 0.000 claims description 8
- 239000003002 pH adjusting agent Substances 0.000 claims description 2
- 108060004795 Methyltransferase Proteins 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 abstract description 31
- -1 beta-glucan compound Chemical class 0.000 abstract description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 abstract description 2
- 108010064851 Plant Proteins Proteins 0.000 abstract description 2
- 235000021118 plant-derived protein Nutrition 0.000 abstract description 2
- 238000001556 precipitation Methods 0.000 abstract description 2
- 239000000243 solution Substances 0.000 description 40
- 229920001282 polysaccharide Polymers 0.000 description 13
- 239000005017 polysaccharide Substances 0.000 description 13
- 150000004676 glycans Chemical class 0.000 description 12
- 229940071440 soy protein isolate Drugs 0.000 description 12
- 108010082495 Dietary Plant Proteins Proteins 0.000 description 9
- 239000000839 emulsion Substances 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- 239000008055 phosphate buffer solution Substances 0.000 description 8
- 230000000052 comparative effect Effects 0.000 description 7
- 238000004945 emulsification Methods 0.000 description 7
- 230000001804 emulsifying effect Effects 0.000 description 7
- 230000036571 hydration Effects 0.000 description 7
- 238000006703 hydration reaction Methods 0.000 description 7
- 125000001165 hydrophobic group Chemical group 0.000 description 7
- 229920001503 Glucan Polymers 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 235000013305 food Nutrition 0.000 description 5
- 235000019198 oils Nutrition 0.000 description 5
- 229920001661 Chitosan Polymers 0.000 description 4
- 230000000259 anti-tumor effect Effects 0.000 description 4
- 239000007864 aqueous solution Substances 0.000 description 4
- 150000003384 small molecules Chemical class 0.000 description 4
- 150000001413 amino acids Chemical class 0.000 description 3
- 230000009286 beneficial effect Effects 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 239000003995 emulsifying agent Substances 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 108010016626 Dipeptides Proteins 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000009145 protein modification Effects 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 235000019737 Animal fat Nutrition 0.000 description 1
- 240000001008 Dimocarpus longan Species 0.000 description 1
- 235000000235 Euphoria longan Nutrition 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 238000010170 biological method Methods 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 150000001728 carbonyl compounds Chemical class 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 235000013861 fat-free Nutrition 0.000 description 1
- 235000012041 food component Nutrition 0.000 description 1
- 239000005417 food ingredient Substances 0.000 description 1
- 238000001879 gelation Methods 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 235000013622 meat product Nutrition 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 238000000053 physical method Methods 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000019635 sulfation Effects 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- 235000020238 sunflower seed Nutrition 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- 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
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/185—Vegetable proteins
-
- 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
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/125—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives containing carbohydrate syrups; containing sugars; containing sugar alcohols; containing starch hydrolysates
-
- 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
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/14—Yeasts or derivatives thereof
-
- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08B—POLYSACCHARIDES; DERIVATIVES THEREOF
- C08B37/00—Preparation of polysaccharides not provided for in groups C08B1/00 - C08B35/00; Derivatives thereof
- C08B37/0006—Homoglycans, i.e. polysaccharides having a main chain consisting of one single sugar, e.g. colominic acid
- C08B37/0024—Homoglycans, i.e. polysaccharides having a main chain consisting of one single sugar, e.g. colominic acid beta-D-Glucans; (beta-1,3)-D-Glucans, e.g. paramylon, coriolan, sclerotan, pachyman, callose, scleroglucan, schizophyllan, laminaran, lentinan or curdlan; (beta-1,6)-D-Glucans, e.g. pustulan; (beta-1,4)-D-Glucans; (beta-1,3)(beta-1,4)-D-Glucans, e.g. lichenan; Derivatives thereof
-
- 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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- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Polymers & Plastics (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Materials Engineering (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Abstract
The invention discloses a method for improving the emulsibility of yeast soluble beta-glucan, which comprises the following steps: dissolving yeast beta-glucan in deionized water, and performing enzymolysis, centrifugation, alcohol precipitation and freeze-drying treatment to obtain yeast soluble beta-glucan; step two, respectively preparing a yeast soluble beta-glucan buffer solution and a plant protein buffer solution, and mixing to ensure that the mass ratio of the yeast soluble beta-glucan to the peanut protein isolate in the mixed solution is 1-5: 1; and step three, adjusting the pH value of the mixed solution to 8-10, uniformly stirring and hydrating overnight, carrying out damp-heat treatment at 70-95 ℃ for 60-180min, and rapidly carrying out ice bath to finish the reaction to obtain the compound. The invention forms the peanut protein isolate-soluble beta-glucan compound through the Maillard reaction, thereby improving the emulsibility of the peanut protein isolate-soluble beta-glucan compound.
Description
Technical Field
The present invention relates to the field of food processing. More particularly, the invention relates to a method for improving the emulsifiability of yeast soluble beta-glucan.
Background
The yeast beta-glucan is positioned in the inner layer of a yeast cell wall, takes beta-1, 3 glycosidic bonds as a main chain and beta-1, 6 glycosidic bonds as a branched chain, and has a structural formula
It has water retention property and immunityRegulating, antibacterial, antiinflammatory, and antitumor effects. The Chinese ministry of health has approved beta-glucan as a new resource food, the European Food Safety Association (EFSA) has approved beta-glucan preparation as a new resource food ingredient, and the U.S. food and drug administration awards the beta-glucan as a generally recognized safe status, but the application range of the beta-glucan is still limited due to the problem of poor emulsifiability.
Polysaccharide and protein are two important natural emulsifiers, and compared with the synthetic emulsifier, the natural emulsifier has a slower speed of transferring to an oil-water interface, but has a better emulsion stabilizing effect.
There are many reports on modification of polysaccharides to improve emulsibility at home and abroad, including three methods of physical, chemical and biological modification. The physical method mainly comprises irradiation, heating and the like, the chemical method comprises acetylation, sulfation, protein-polysaccharide interaction and the like, and the biological method mainly comprises enzymolysis modification. Among these methods, maillard reaction has attracted increasing attention as a nonenzymatic browning reaction widely occurring in the food industry, which can improve not only emulsifiability of protein but also foamability, gelation property, and the like. Proteins are mainly produced by a reaction between a carbonyl compound (reducing sugar) and an amino compound (protein and amino acid), and the reducing sugar is usually selected as a substrate for the maillard reaction because it has a small molecule, is more likely to contact with an amino group of a protein, and is more likely to occur. However, since yeast beta-glucan has a triple helix structure, it is extremely insoluble in aqueous solutions or most solvents, and it is difficult to graft protein in aqueous solution systems, and thus it is not suitable for protein modification. In addition, small molecule reducing sugar is grafted to protein molecules with large molecular weight due to small molecular weight, and little attention is paid to the change of the structure of the small molecule reducing sugar, but the polysaccharide has large molecular weight, and the structures of two molecules are changed when two substances with large molecular weight are combined. The polysaccharide contains more hydrophilic groups but lacks hydrophobic groups, so that the emulsibility is poor, but the emulsifying property of the Maillard reaction is obviously improved to a certain extent due to the increase of the number of the hydrophobic groups in the molecule, but the property change of the polysaccharide is rarely concerned.
In the existing Maillard reaction research, the functional property of the protein is improved, the reaction between the multi-choice protein and the micromolecule sugar is improved, and the balance between hydrophilic groups and hydrophobic groups in the protein molecules is improved due to the addition of hydrophilic groups in the micromolecule sugar. And polysaccharide modification, more choices are to graft small molecules such as amino acid, dipeptide and the like onto macromolecular polysaccharide, increase hydrophobic groups in polysaccharide molecules, improve the balance of hydrophilic and hydrophobic groups of polysaccharide, and pay attention to the structural change of polysaccharide after the polysaccharide reacts with amino acid and dipeptide. Researches show that a compound formed by reacting longan pulp polysaccharide with lysine has antioxidant, antitumor and immunostimulating activities, while protein modification is more applied to an emulsion loading system, and the bioactivity such as antitumor activity and the like is rarely reported. In addition, the carbohydrate can stabilize water molecules in a fat-free system to form a three-dimensional reticular gel matrix, has animal-like lubricity and fluidity, and has good cohesiveness and water-retaining property when replacing meat products prepared by animals. Carbohydrate raw materials have been approved by the U.S. food and drug administration as "generally recognized safe materials".
Disclosure of Invention
An object of the present invention is to solve at least the above problems and to provide at least the advantages described later.
It is still another object of the present invention to provide a method for improving the emulsifiability of yeast-soluble β -glucan by forming a peanut protein isolate-soluble β -glucan complex by maillard reaction, thereby improving the emulsifiability thereof.
To achieve these objects and other advantages in accordance with the present invention, there is provided a method for improving emulsifiability of yeast soluble β -glucan, comprising:
dissolving yeast beta-glucan in deionized water, and performing enzymolysis, centrifugation, alcohol precipitation and freeze-drying treatment to obtain yeast soluble beta-glucan;
step two, respectively preparing a yeast soluble beta-glucan buffer solution and a plant protein buffer solution, and mixing to ensure that the mass ratio of the yeast soluble beta-glucan to the peanut protein isolate in the mixed solution is 1-5: 1;
and step three, adjusting the pH value of the mixed solution to 8-10, uniformly stirring and hydrating overnight, carrying out damp-heat treatment at 70-95 ℃ for 60-180min, and rapidly carrying out ice bath to finish the reaction to obtain the compound.
Preferably, the vegetable protein is a peanut protein isolate.
Preferably, the concentration of the yeast soluble β -glucan buffer solution is 6-30 mg/mL.
Preferably, the concentration of the peanut protein isolate buffer solution is 2-10 mg/mL.
Preferably, hydrochloric acid or sodium hydroxide is used as a pH adjuster for adjusting the pH.
Preferably, the molar concentration of hydrochloric acid or sodium hydroxide is 1 to 5 mol/mL.
Preferably, the first step is specifically: s1: dissolving yeast beta-glucan in deionized water to prepare a suspension with the mass fraction of 1.5%, and preheating the suspension in a water bath kettle at 45 ℃;
s2: adding 4% snailase into the suspension, preheating for 5min, and shaking for hydrolysis for 80 min;
s3: inactivating enzyme in boiling water bath for 10min, centrifuging, collecting supernatant, and lyophilizing.
The yeast soluble beta-glucan-peanut isolated protein compound obtained by the method.
The yeast soluble beta-glucan-peanut protein isolate compound obtained by the method is applied to the field of food.
Preferably, the yeast soluble β -glucan-peanut isolate complex replaces animal fat.
The invention at least comprises the following beneficial effects:
the invention takes yeast beta-glucan and vegetable protein as raw materials to prepare the vegetable protein-soluble beta-glucan compound, thereby improving the emulsibility of the compound.
Additional advantages, objects, and features of the invention will be set forth in part in the description which follows and in part will become apparent to those having ordinary skill in the art upon examination of the following or may be learned from practice of the invention.
Detailed Description
The present invention is further described in detail below with reference to examples to enable those skilled in the art to practice the invention with reference to the description.
It will be understood that terms such as "having," "including," and "comprising," as used herein, do not preclude the presence or addition of one or more other elements or groups thereof.
It is to be noted that the experimental methods described in the following embodiments are all conventional methods unless otherwise specified, and the reagents and materials are commercially available unless otherwise specified.
< example 1>
A method of improving the emulsifiability of yeast soluble β -glucan comprising:
(1) dissolving yeast beta-mother glucan in deionized water to prepare a suspension with the mass fraction of 1.5%, and preheating the suspension in a 45-turbidity water bath; adding 4% snailase into the suspension, preheating for 5min, and shaking for hydrolysis for 80 min; inactivating enzyme in boiling water bath for 10min, centrifuging, collecting supernatant, and lyophilizing to obtain yeast soluble beta-glucan;
(2) dissolving peanut protein isolate and yeast soluble beta-glucan in phosphate buffer solution to obtain 10mg/mL peanut protein isolate and 30mg/mL yeast soluble beta-glucan solution respectively;
(3) mixing a yeast soluble beta-glucan solution and a peanut protein isolate solution according to a solute mass ratio of 1:1, adjusting the pH of the mixture solution to 10, uniformly stirring and hydrating for overnight;
(4) after hydration, the solution is subjected to moist heat treatment at 70 ℃ for 60min, and the reaction is finished by rapid ice-bath.
< example 2>
A method of improving the emulsifiability of yeast soluble β -glucan comprising:
(1) dissolving yeast beta-mother glucan in deionized water to prepare a suspension with the mass fraction of 1.5%, and preheating the suspension in a 45-turbidity water bath; adding 4% snailase into the suspension, preheating for 5min, and shaking for hydrolysis for 80 min; inactivating enzyme in boiling water bath for 10min, centrifuging, collecting supernatant, and lyophilizing to obtain yeast soluble beta-glucan;
(2) dissolving peanut protein isolate and yeast-soluble beta-glucan in phosphate buffer solution to obtain 6mg/mL peanut protein isolate and 18mg/mL yeast-soluble beta-glucan solution respectively;
(3) mixing a yeast soluble beta-glucan solution and a peanut protein isolate solution according to a solute mass ratio of 5:1, adjusting the pH of the mixture solution to 9, uniformly stirring, and hydrating overnight;
(4) after hydration, the solution is subjected to moist heat treatment at 80 ℃ for 60min, and the reaction is finished by rapidly cooling in an ice bath.
< example 3>
A method of improving the emulsifiability of yeast soluble β -glucan comprising:
(1) dissolving yeast beta-mother glucan in deionized water to prepare a suspension with the mass fraction of 1.5%, and preheating the suspension in a 45-turbidity water bath; adding 4% snailase into the suspension, preheating for 5min, and shaking for hydrolysis for 80 min; inactivating enzyme in boiling water bath for 10min, centrifuging, collecting supernatant, and lyophilizing to obtain yeast soluble beta-glucan;
(2) dissolving peanut protein isolate and yeast-soluble beta-glucan in phosphate buffer solution to obtain 2mg/mL peanut protein isolate and 6mg/mL yeast-soluble beta-glucan solution respectively;
(3) mixing a yeast soluble beta-glucan solution and a peanut protein isolate solution according to a solute mass ratio of 3:1, adjusting the pH of the mixture solution to 9, uniformly stirring and hydrating overnight;
(4) after hydration, the solution is subjected to moist heat treatment at 90 ℃ for 80min, and the reaction is finished by rapid ice bath.
< example 4>
A method of improving the emulsifiability of yeast soluble β -glucan comprising:
(1) dissolving yeast beta-mother glucan in deionized water to prepare a suspension with the mass fraction of 1.5%, and preheating the suspension in a 45-turbidity water bath; adding 4% snailase into the suspension, preheating for 5min, and shaking for hydrolysis for 80 min; inactivating enzyme in boiling water bath for 10min, centrifuging, collecting supernatant, and lyophilizing to obtain yeast soluble beta-glucan;
(2) dissolving the soy protein isolate and the yeast soluble beta-glucan in a phosphate buffer solution to obtain 6mg/mL soy protein isolate and 18mg/mL yeast soluble beta-glucan solution respectively;
(3) mixing a yeast soluble beta-glucan solution and a soy protein isolate solution according to a solute mass ratio of 3:1, adjusting the pH of the mixture solution to 10, uniformly stirring and hydrating overnight;
(4) after hydration, the solution is subjected to moist heat treatment at 95 ℃ for 60min, and the reaction is finished by rapid ice-bath.
< example 5>
A method of improving the emulsifiability of yeast soluble β -glucan comprising:
(1) dissolving yeast beta-mother glucan in deionized water to prepare a suspension with the mass fraction of 1.5%, and preheating the suspension in a 45-turbidity water bath; adding 4% snailase into the suspension, preheating for 5min, and shaking for hydrolysis for 80 min; inactivating enzyme in boiling water bath for 10min, centrifuging, collecting supernatant, and lyophilizing to obtain yeast soluble beta-glucan;
(2) dissolving the soy protein isolate and the yeast-soluble beta-glucan in a phosphate buffer solution to obtain 2mg/mL soy protein isolate and 6mg/mL yeast-soluble beta-glucan solution respectively;
(3) mixing a yeast soluble beta-glucan solution and a soy protein isolate solution according to a solute mass ratio of 3:1, adjusting the pH of the mixture solution to 9, uniformly stirring and hydrating overnight;
(4) after hydration, the solution is subjected to moist heat treatment at 90 ℃ for 180min, and the reaction is finished by rapid ice-bath.
< comparative example 1>
(1) Dissolving yeast beta-mother glucan in deionized water to prepare a suspension with the mass fraction of 1.5%, and preheating the suspension in a 45-turbidity water bath; adding 4% snailase into the suspension, preheating for 5min, and shaking for hydrolysis for 80 min; inactivating enzyme in boiling water bath for 10min, centrifuging, collecting supernatant, and lyophilizing to obtain yeast soluble beta-glucan;
(2) dissolving yeast soluble beta-glucan in a phosphate buffer solution to obtain a 6mg/mL yeast soluble beta-glucan solution;
(3) adjusting the pH value of the yeast soluble beta-glucan solution to 9, uniformly stirring and standing overnight;
(4) the solution was heat-wet treated at 90 ℃ for 60 min.
< comparative example 2>
(1) Dissolving the soy protein isolate and the yeast beta-glucan in a phosphate buffer solution to obtain 6mg/mL soy protein isolate and 18mg/mL yeast beta-glucan solution respectively;
(2) mixing a yeast beta-glucan solution and a soy protein isolate solution according to a solute mass ratio of 3:1, adjusting the pH of the mixture solution to 10, uniformly stirring and hydrating for overnight;
(3) after hydration, the solution is subjected to moist heat treatment at 95 ℃ for 60min, and the reaction is finished by rapid ice-bath.
< comparative example 3>
(1) Dissolving soy protein isolate and chitosan in phosphate buffer solution to obtain 6mg/mL soy protein isolate and 18mg/mL chitosan solution respectively;
(2) mixing a chitosan solution and a soy protein isolate solution according to a solute mass ratio of 3:1, adjusting the pH of the mixture solution to 10, uniformly stirring and hydrating overnight;
(3) after hydration, the solution is subjected to moist heat treatment at 95 ℃ for 60min, and the reaction is finished by rapid ice-bath.
< test on emulsification Property >
Method for measuring emulsifiability
Adding 3mL sunflower seed oil into 7mL reacted compound solution, homogenizing at 1000rpm for 2min, quickly adding 50 μ L emulsion from bottom into 5mL 0.1% SDS solution, and measuring absorbance at 500nm as A0And measuring the absorbance again after 10min and recording as A1The calculation formula of emulsifiability and emulsion stability is as follows:
emulsion active EAI (m)2/g)＝2×2.303×A0×D/(C×Φ×L×104)
Emulsion stability ESI (min) ═ A0×10/(A0-A10)
Wherein D is the dilution multiple, namely 100;
c is the concentration of protein
L is the optical path of the cuvette, i.e. 1cm
Phi is the oil phase ratio
The emulsibility is the capacity of oil and water to form emulsion, and comprises two indexes of emulsification activity and emulsification stability, wherein the emulsification activity refers to the stability of the oil-water interface area of a unit mass sample when oil and water are mixed; the emulsification stability refers to the ability of maintaining the emulsification characteristic of not separating oil and water mixture to resist strain to the outside, and the two indexes represent different aspects of the emulsification.
The emulsifiability of the complexes prepared in examples 1 to 5 and comparative examples 1 to 3 was compared, and the results are shown in the table:
TABLE 1 emulsifiability comparison results
As can be seen from the above table, compared with the emulsifying property without adding vegetable protein in comparative example 1, the emulsifying activity and the emulsifying stability with the addition of vegetable protein are significantly improved, because the addition of vegetable protein increases the number of hydrophobic groups in the system, which is beneficial to the balance of hydrophilic groups and hydrophobic groups, and in addition, the improvement of the emulsifying activity in examples 1, 2 and 4 is inferior to that in examples 3 and 5, but the emulsifying stability is higher, which indicates that it has better ability to stabilize the emulsion; compared with the direct combination of the yeast beta-glucan and the vegetable protein in the comparative example 2, the yeast beta-glucan has better emulsibility after being subjected to enzymolysis and then reacting with the vegetable protein, because the molecular weight and the particle size of the yeast beta-glucan are slightly reduced after the yeast beta-glucan is subjected to the enzymolysis, but the yeast beta-glucan still has larger molecular weight and a highly ordered structure, and researches show that the modified water-soluble beta-glucan still has antitumor activity. On the premise of not changing the physiological activity, the solubility of the soluble beta-glucan in an aqueous solution system is increased, the structure of the protein is expanded after heating treatment, and the flexibility of the soluble beta-glucan in the aqueous solution is increased, so that the soluble beta-glucan is more beneficial to the contact and combination with the vegetable protein. Comparative example 3 the emulsifying properties of chitosan and vegetable protein treated in the same manner were also inferior to those of the soluble β -glucan-vegetable protein complex.
The number of apparatuses and the scale of the process described herein are intended to simplify the description of the present invention. Applications, modifications and variations of the present invention will be apparent to those skilled in the art.
While embodiments of the invention have been disclosed above, it is not limited to the applications set forth in the description and the embodiments, which are fully applicable in various fields of endeavor to which the invention pertains, and further modifications may readily be made by those skilled in the art, it being understood that the invention is not limited to the details shown and described herein without departing from the general concept defined by the appended claims and their equivalents.
Claims (3)
1. A method for improving the emulsifiability of yeast soluble β -glucan, comprising:
dissolving yeast beta-glucan in deionized water, and performing enzymolysis, centrifugation and freeze-drying treatment to obtain yeast soluble beta-glucan;
the first step is specifically as follows: s1: dissolving yeast beta-glucan in deionized water to prepare a suspension with the mass fraction of 1.5%, and preheating the suspension in a water bath kettle at 45 ℃;
s2: adding helicase 4% into the suspension, preheating for 5min, and shaking for hydrolysis for 80 min;
s3: inactivating enzyme in boiling water bath for 10min, centrifuging, collecting supernatant, and lyophilizing;
step two, respectively preparing a yeast soluble beta-glucan buffer solution and a peanut protein isolate buffer solution, and mixing to ensure that the mass ratio of the yeast soluble beta-glucan to the peanut protein isolate in the mixed solution is 1-5: 1;
step three, adjusting the pH value of the mixed solution to 8-10, uniformly stirring and hydrating for overnight, carrying out damp-heat treatment at 70-95 ℃ for 60-180min, and rapidly carrying out ice bath to finish the reaction to obtain the compound;
the concentration of the yeast soluble beta-glucan buffer solution is 6-30 mg/mL;
the concentration of the peanut protein isolate buffer solution is 2-10 mg/mL.
2. The method for improving the emulsifiability of yeast-soluble β -glucan according to claim 1, wherein the pH is adjusted by using hydrochloric acid or sodium hydroxide as a pH adjuster.
3. The method for improving the emulsifiability of yeast-soluble β -glucan according to claim 2, wherein the molar concentration of hydrochloric acid or sodium hydroxide is 1 to 5 mol/mL.
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