WO2022210752A1 - 変性タンパク質素材 - Google Patents
変性タンパク質素材 Download PDFInfo
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- WO2022210752A1 WO2022210752A1 PCT/JP2022/015616 JP2022015616W WO2022210752A1 WO 2022210752 A1 WO2022210752 A1 WO 2022210752A1 JP 2022015616 W JP2022015616 W JP 2022015616W WO 2022210752 A1 WO2022210752 A1 WO 2022210752A1
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- Prior art keywords
- protein
- protein material
- denatured protein
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- denatured
- Prior art date
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- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 167
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 167
- 239000000463 material Substances 0.000 title claims abstract description 131
- 238000009826 distribution Methods 0.000 claims abstract description 44
- 239000007864 aqueous solution Substances 0.000 claims abstract description 36
- 229960000789 guanidine hydrochloride Drugs 0.000 claims abstract description 19
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 claims abstract description 19
- 235000019750 Crude protein Nutrition 0.000 claims abstract description 17
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims abstract description 16
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims abstract description 16
- 235000011130 ammonium sulphate Nutrition 0.000 claims abstract description 16
- 235000018102 proteins Nutrition 0.000 claims description 164
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- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
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Images
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
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/10—Foods or foodstuffs containing additives; Preparation or treatment thereof containing emulsifiers
-
- 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
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
-
- 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
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C11/00—Milk substitutes, e.g. coffee whitener compositions
- A23C11/02—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins
- A23C11/10—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins
- A23C11/103—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins containing only proteins from pulses, oilseeds or nuts, e.g. nut milk
-
- 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
- A23V2200/00—Function of food ingredients
- A23V2200/20—Ingredients acting on or related to the structure
- A23V2200/222—Emulsifier
Definitions
- the present invention relates to a denatured protein material and a method for producing the same.
- sodium caseinate and the like are used as proteins with emulsifying power.
- Synthetic emulsifiers such as glycerin fatty acid esters are used when further emulsifying power is required.
- sodium caseinate which is widely used as a protein having emulsifying power, is a milk protein, that is, an animal protein. At present, due to concerns about food supply due to population growth, attempts are being made to reduce the amount of animal protein and to replace foods using animal protein with foods using vegetable protein.
- milk protein if the amount of milk protein is reduced, the effect may not be sufficiently obtained.
- vegetable proteins such as soybean protein and pea protein are generally inferior to milk proteins in terms of high viscosity when made into a solution, solubility, mineral resistance, and heat resistance such as retort heating. Problems such as thickening and generation of agglomerates tend to occur, and the amount to be blended is limited. Therefore, at present, it is not used as a substitute for milk protein.
- Patent Literature 1 provides a technique of enzymatic decomposition while adding reducing sugar to isolated soy protein and heat-treating it to promote the Maillard reaction.
- Patent Document 2 provides a technique of heat-treating proteins at 140° C. for about 30 seconds, enzymatically decomposing them, and then adding fats and oils.
- Patent Document 3 discloses an emulsified composition in which a specific vegetable protein material, fat and oil, and optionally carbohydrate are mixed in a specific ratio. These are intended to improve the viscosity and emulsifying power while maintaining the solubility of the protein by improving the vegetable protein material.
- An object of the present invention is to provide a protein material with improved emulsifying power.
- the denatured protein material of (1) wherein the area ratio of less than 2,000 Da is 45% or less as a result of measuring the molecular weight distribution; (3) The denatured protein material of (1), wherein the area ratio of 10,000 Da or more is less than 50% as a result of measuring the molecular weight distribution; (4) The denatured protein material of (1), whose molecular weight distribution measurement results show that the area ratio of less than 2,000 Da is 45% or less and the area ratio of 10,000 Da or more is less than 50%; (5) The denatured protein material of (1), wherein the denatured protein material has an OD660nm of 0.5 or less in an aqueous solution prepared to have a protein content of 10% by mass and a pH of 7; (6) The denatured protein material of (4), wherein the denatured protein material has an aqueous solution prepared to have a protein content of 10% by mass and a pH of 7, and an OD660nm of 0.5
- a protein material with improved emulsifying power can be provided.
- Emulsified foods with improved emulsion stability can be produced by using the denatured protein material of the present invention.
- an emulsified food having emulsification stability can be produced without using a synthetic emulsifier or the like.
- an emulsified food having emulsification stability can be produced without using an animal protein material.
- by preparing a denatured protein material using milk protein as a raw material it is possible to reduce the amount of milk protein while maintaining emulsifying power.
- FIG. 1 is a chart showing molecular weight distributions of Arg, isolated soybean protein, soybean peptide, enzyme-treated isolated soybean protein described in Test Examples 1 and 2, and the protein material of Patent Document 3.
- the vertical axis indicates intensity ( ⁇ V), and the horizontal axis indicates retention time (minutes). Vertical lines in the figure indicate positions of 20,000 Da, 10,000 Da, and 2,000 Da from the left.
- FIG. 2 is a chart showing the molecular weight distribution of denatured protein materials A to E described in Example 1.
- FIG. The vertical axis indicates intensity ( ⁇ V), and the horizontal axis indicates retention time (minutes). Vertical lines in the figure indicate positions of 20,000 Da, 10,000 Da, and 2,000 Da from the left.
- a denatured protein material which is one aspect of the present invention, is characterized by the following. a) The area ratio of 2,000 Da or more and less than 20,000 Da is 45 to 90% in the results of molecular weight distribution measurement, and b) No cloudiness when 250 mM guanidine hydrochloride is added to an aqueous solution of denatured protein material with a crude protein concentration of 0.1%. , turns cloudy when 2M ammonium sulfate is added.
- the present invention provides a denatured protein material.
- a method for producing a denatured protein material is provided.
- a food product comprising the denatured protein material is provided.
- a composition comprising a denatured protein material is provided.
- protein material is a food material that has protein as its main component and is used as a raw material in various processed foods and beverages.
- denatured protein material refers to a food material containing denatured protein as a main component.
- the protein from which the denatured protein material of the present disclosure is derived may be animal protein, vegetable protein, or a mixture thereof.
- animal proteins include proteins derived from cows, pigs, chickens, eggs and milk.
- vegetable proteins include legumes such as soybeans, peas, mung beans, fava beans, lupine beans, chickpeas, kidney beans, lentils, and cowpeas; seeds such as sesame seeds, canola seeds, coconut seeds and almond seeds; corn and buckwheat. , grains such as wheat and rice, vegetables, and fruits.
- the denatured protein material of this aspect 50% by mass or more of the protein is derived from vegetable protein, for example, 55% by mass or more, 60% by mass or more, 65% by mass or more, 70% by mass or more, 75% by mass. % or more, 80% or more, 85% or more, 90% or more, 95% or more, or 97% or more by weight can be derived from vegetable proteins, most preferably 100% by weight or more is.
- the denatured protein material does not include protein material derived from milk proteins.
- the denatured protein material is prepared from legume protein.
- the denatured protein material is prepared from soy protein, pea protein, mung bean protein or fava bean protein.
- soybean-derived protein material it is prepared by further concentrating protein from soybean raw materials such as defatted soybeans and whole soybeans.
- Various processed products are conceptually included.
- the area ratio of the molecular weight distribution is 45 to 90%, for example, 50 to 85%, 55 to 2,000 Da or more and less than 20,000 Da. ⁇ 80%, 55-75%, 60-70%.
- the protein material described in Patent Document 3 has an area ratio of 20,000 Da or more exceeding 55%, and is different from the denatured protein material of the present disclosure in this respect.
- the area percentage of less than 2,000 Da is 45% or less, such as 40% or less, 35% or less, 30% or less, 25% or less.
- the lower limit is not particularly limited, examples thereof include 0% or more, 1% or more, 2% or more, 5% or more, 10% or more, and 15% or more.
- the area percentage of 10,000 Da or more is less than 50%, such as 5-45%, 10-40%, 15-35%.
- the area percentage of 20,000 Da or greater is less than 55%, such as 50% or less, 40% or less, 30% or less, 25% or less, 20% or less, 15% or less.
- the molecular weight distribution of the denatured protein material is in such a range indicates that the main component is moderately low molecular weight, while the undegraded protein that has not been subjected to any decomposition treatment It shows that there are few degraded small peptides.
- the measurement of molecular weight distribution shall be based on the method mentioned later.
- the addition of guanidine hydrochloride to prevent clouding means that an aqueous solution with a crude protein concentration of 0.1% and a 250 mM guanidine hydrochloride does not have clouding visually, or the OD660nm of the aqueous solution is less than 0.3, for example, 0.2 or less, 0.1 or less, It can be confirmed by being 0.
- the denatured protein material of the present disclosure becomes cloudy when ammonium sulfate is added to the aqueous solution. This is an index indicating that the protein has a certain degree of polymerization and is not an excessively degraded peptide such as dipeptide or tripeptide.
- adding ammonium sulfate to make it cloudy means visually observing cloudiness in an aqueous solution of 2M ammonium sulfate with a crude protein concentration of 0.1%, or the OD660nm of the aqueous solution is 0.3 or more, for example, 0.4 or more, 0.5 or more.
- the procedures for adding guanidine hydrochloride and ammonium sulfate are based on the method described later.
- the denatured protein material of the present disclosure satisfies the above a) to b). Although not particularly limited, the characteristics of the denatured protein material in more specific embodiments will be described below.
- the denatured protein material of the present disclosure preferably has a protein content of 40% by mass or more in solid content, for example, 50% by mass or more, 60% by mass or more, 70% by mass or more. % or more, 80 mass % or more, 85 mass % or more, or 90 mass % or more.
- a raw material for the denatured protein material within the above range isolated protein is preferable.
- soymilk-level protein content is low, it becomes necessary to add a large amount of denatured protein material in order to produce an emulsified food with a high protein content, which may impair its versatility as a material.
- Viscosity when the viscosity of the denatured protein material solution of the present disclosure is measured under constant conditions, it is preferably low viscosity. It preferably has a viscosity of 50 mPa ⁇ s or less at 60° C., for example, 40 mPa ⁇ s or less, 35 mPa ⁇ s or less, 30 mPa ⁇ s or less, 20 mPa ⁇ s or less, 15 mPa ⁇ s or less, 10 mPa ⁇ s or less, or 5 mPa ⁇ s or less.
- the lower limit of the viscosity is not particularly limited, but examples thereof include 0.1 mPa ⁇ s or more, 0.5 mPa ⁇ s or more, and 1 mPa ⁇ s or more.
- the viscosity is measured by the method described later.
- the denatured protein material of the present disclosure has a solubility in water at room temperature of 20 wt% or greater, such as 25 wt% or greater.
- the upper limit of the solubility is not particularly limited, examples thereof include 55% by mass or less, 50% by mass or less, 45% by mass or less, 40% by mass or less, and 35% by mass or less.
- the aqueous solution of the denatured protein material of the present disclosure is preferably less turbid, more preferably clear. More specifically, a 10% aqueous solution (pH 7) of the denatured protein material of the present disclosure is prepared, and the value of OD660 nm at room temperature after standing overnight is preferably 0.5 or less, for example, 0.3 or less, 0.2 or less, or 0.1. 0 below.
- the denatured protein material of the present disclosure meets the numerical values specified by e) solubility and/or f) turbidity above, and is therefore also referred to as a "water-soluble denatured protein material.” be.
- the median diameter of the emulsion containing the denatured protein material of the present disclosure is 4 ⁇ m or less, such as 3 ⁇ m or less, 2 ⁇ m or less, 1 ⁇ m or less. More specifically, an emulsion containing the denatured protein material of the present disclosure with a crude protein content of 1% or more, for example, 0.5% or more, 0.1% or more, or 0.05% or more exhibits the above median diameter. Preparation of the emulsion and measurement of the median diameter shall be based on the method described later.
- the denatured protein material of the present disclosure can be obtained by combining protein denaturation and molecular weight distribution adjustment.
- protein denaturation treatment include pH adjustment treatment (e.g., acid treatment, alkali treatment), denaturant treatment, heat treatment, cooling treatment, high pressure treatment, organic solvent treatment, mineral addition treatment, supercritical treatment, and ultrasonic treatment. , electrolysis, and combinations thereof.
- treatments for adjusting the molecular weight distribution include enzymatic treatment, filtration, gel filtration, chromatography, centrifugation, electrophoresis, dialysis, combinations thereof, and the like.
- the order and number of times of the treatment for denaturing the protein and the treatment for adjusting the molecular weight distribution are not particularly limited, and the treatment for denaturing the protein may be followed by the treatment for adjusting the molecular weight distribution, or the molecular weight distribution may be adjusted.
- a treatment for denaturing the protein may be performed after the treatment, or both treatments may be performed at the same time. Further, for example, a treatment for denaturing the protein is performed between two or more treatments for adjusting the molecular weight distribution, a treatment for adjusting the molecular weight distribution is performed between two or more treatments for denaturing the protein, and each treatment is performed multiple times. can be performed in any order.
- the treatment for adjusting the molecular weight distribution may not be performed.
- all the treatments starting from the raw material may be carried out continuously, or may be carried out after an interval of time.
- a commercial product that has undergone a certain treatment may be used as a raw material and subjected to another treatment.
- such treatment is referred to as "denaturation/molecular weight distribution adjustment treatment" for convenience.
- a specific denatured protein material may be obtained by mixing a denatured protein material that has undergone denaturation/molecular weight distribution adjustment treatment and a protein that has not undergone denaturation/molecular weight distribution adjustment treatment.
- the ratio of the two protein material that has undergone denaturation/molecular weight distribution adjustment treatment: protein that has not undergone denaturation/molecular weight distribution adjustment treatment
- the denatured protein material of the present disclosure consists of a vegetable protein material that has undergone denaturation and molecular weight distribution control treatment.
- a person skilled in the art can appropriately set the conditions of the protein denaturation treatment, such as the concentrations of acids, alkalis, organic solvents, minerals, etc., temperature, pressure, output intensity, current, time, etc.
- pH adjustment treatment any of pH 2, 2.5, 3, 3.5, 4, 4.5, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9, 9.5, 10, 10.5, 11, 11.5, 12 can be treated in a pH range with upper and lower limits, eg, pH 2-12.
- acid treatment it may be a method of adding acid or a method of carrying out fermentation treatment such as lactic acid fermentation.
- acids to be added include inorganic acids such as hydrochloric acid and phosphoric acid; Organic acids are mentioned.
- acid may be added using acid-containing foods and drinks such as fruit juice such as lemon, concentrated fruit juice, fermented milk, yogurt, and brewed vinegar.
- alkali treatment an alkali such as sodium hydroxide or potassium hydroxide can be added.
- denaturants such as guanidine hydrochloride, urea, arginine, PEG, etc. may be added.
- heating or cooling treatment examples of heating temperatures are 60°C, 70°C, 80°C, 90°C, 100°C, 110°C, 120°C, 125°C, 130°C, 135°C, 140°C, 145°C, and 150°C.
- °C the upper limit and the lower limit of which are, for example, 60°C to 150°C.
- cooling temperatures are -10°C, -15°C, -20°C, -25°C, -30°C, -35°C, -40°C, -45°C, -50°C, -55°C, -60°C, Ranges with upper and lower limits of -65°C, -70°C, and -75°C, such as -10°C to -75°C.
- heating or cooling times are 5 seconds, 10 seconds, 30 seconds, 1 minute, 5 minutes, 10 minutes, 20 minutes, 30 minutes, 40 minutes, 50 minutes, 60 minutes, 70 minutes, 80 minutes, 90 minutes, Ranges with upper and lower limits of 100 minutes, 120 minutes, 150 minutes, 180 minutes, and 200 minutes, such as 5 seconds to 200 minutes.
- examples of pressure conditions are 100 MPa, 200 MPa, 300 MPa, 400 MPa, 500 MPa, 600 MPa, 700 MPa, 800 MPa, 900 MPa, and 1,000 MPa. mentioned.
- examples of solvents used include alcohols and ketones such as ethanol and acetone.
- examples of minerals used include divalent metal ions such as calcium and magnesium.
- ⁇ for example, carbon dioxide in a supercritical state at a temperature of about 30° C. or higher and about 7 MPa or higher can be used.
- ultrasonic treatment for example, treatment can be performed by irradiating with a frequency of 100 KHz to 2 MHz and an output of 100 to 1,000 W.
- electrolysis treatment for example, a protein aqueous solution can be treated by applying a voltage of 100 mV to 1,000 mV.
- the treatment that denatures the protein is selected from denaturant treatment, heat treatment, and combinations thereof.
- a person skilled in the art can appropriately set the processing conditions for adjusting the molecular weight distribution, such as enzymes, types of filter media, number of revolutions, electric current, and time.
- enzymes that may be used include proteases classified as “metalloproteases,” “acid proteases,” “thiol proteases,” and “serine proteases.”
- the reaction temperature is 20 to 80°C, preferably 40 to 60°C.
- filter media include filter paper, filter cloth, diatomaceous earth, ceramics, glass, membranes, and the like.
- carriers for gel filtration include dextran and agarose.
- centrifugation conditions include 1,000 to 3,000 G for 5 to 20 minutes.
- ingredients may or may not be added to the denatured protein material of the present disclosure as long as it does not impair its function.
- examples of other raw materials include seasonings, acidulants, sweeteners, spices, colorants, flavors, salts, sugars, antioxidants, vitamins, stabilizers, thickeners, carriers, excipients, lubricants, and interfaces. Active agents, propellants, preservatives, chelating agents, pH adjusters, and the like. It should be noted that, in specific embodiments, the denatured protein material of the present disclosure does not contain animal-derived components.
- the form of the denatured protein material of the present disclosure is not particularly limited, and examples include solids such as powders, granules, and pellets, semisolids such as pastes, and liquids such as solutions, suspensions, and emulsions.
- the denatured protein is a powder, prepared through a drying process such as spray drying, freeze drying, and the like.
- the denatured protein material of the present disclosure can be blended into foods or used as a raw material for compositions. Since the denatured protein material of the present disclosure has improved emulsifying power, it can be suitably used for emulsified foods and emulsified compositions. A person skilled in the art can appropriately select and determine the intended use and amount of addition of the denatured protein material of the present disclosure. In certain embodiments, examples of the added amount of the denatured protein material of the present disclosure are 0.1 to 70% by mass, 0.5 to 60% by mass, 1 to 50% by mass, 5 to 45% by mass, 10 to 40% by mass per food or composition. % by mass.
- the nitrogen conversion factor is 6.25. Basically, it is obtained by rounding off the second decimal place.
- the protein material is adjusted to a concentration of 0.1% by mass with an eluent, and filtered through a 0.2 ⁇ m filter to obtain a sample solution.
- a gel filtration system is assembled by connecting two columns in series, and a known protein or the like (Table 1) serving as a molecular weight marker is first charged, and a calibration curve is obtained from the relationship between molecular weight and retention time.
- the sample solution is charged, and the content ratio % of each molecular weight fraction is determined by the ratio of the area of the specific molecular weight range (time range) to the total absorbance chart area (1st column: “TSK gel G3000SW XL " (SIGMA-ALDRICH), 2nd column: “TSK gel G2000SW XL “ (SIGMA-ALDRICH), eluent: 1% SDS + 1.17% NaCl + 50 mM phosphate buffer (pH 7.0), 23°C, flow rate: 0.4 ml/ min, detection: UV220nm). Basically, it is obtained by rounding off the second decimal place.
- guanidine hydrochloride Prepare an aqueous solution of protein material with a crude protein concentration of 0.2%. If cloudiness occurs during the preparation of an aqueous solution, centrifuge after preparing an aqueous solution of about 1 to 10%, collect the supernatant, dilute to a crude protein concentration of 0.2%, and use it as a sample solution. An equal volume of guanidine hydrochloride solution is added to this to prepare a solution with a crude protein concentration of 0.1% and a guanidine hydrochloride concentration of 250 mM, and allowed to stand overnight in a refrigerator. Check visually for cloudiness. In addition, turbidity is measured at a wavelength of 660 nm using a 10 mm glass cell.
- ⁇ Ammonium sulfate addition> Prepare an aqueous solution of protein material with a crude protein concentration of 0.2%. If cloudiness occurs during the preparation of an aqueous solution, centrifuge after preparing an aqueous solution of about 1 to 10%, collect the supernatant, dilute to a crude protein concentration of 0.2%, and use it as a sample solution. An equal amount of ammonium sulfate solution is added to this to prepare a solution with a crude protein concentration of 0.1% and an ammonium sulfate concentration of 2M, and allowed to stand overnight in a refrigerator. Check visually for cloudiness. In addition, turbidity is measured at a wavelength of 660 nm using a 10 mm glass cell.
- ⁇ Viscosity> For the viscosity of the protein material, prepare an aqueous solution of the protein material so that the protein content is 10% by mass, and measure at 60 ° C with a Brookfield viscometer (preferably Brookfield) using the rotor "#LV-1". and is obtained as the measured value shown after 1 minute at 100 rpm. If it is impossible to measure with "#LV-1", replace the rotor with "#LV-2", “#LV-3", “#LV-4", and "#LV-5".
- Test Example 1 Examination of protein denaturation To an aqueous solution of isolated soy protein (Fuji Oil Co., Ltd.), arginine was added as a denaturant to 0.5M. Then, after heating this aqueous solution at 121° C. for 10 minutes, the denaturant was removed using an MW3500 dialysis tube, followed by freeze-drying to obtain a powdery protein material (referred to as Arg). Arg, MCT64 (medium chain fatty acid oil, Fuji Oil Co., Ltd.), and water were mixed to obtain an oil content of 20% and a crude protein concentration of 1%, 0.5%, 0.1%, and 0.05%, followed by sonication.
- Arg powdery protein material
- An emulsion was prepared by After the prepared emulsion was stored in a refrigerator, the median diameter was measured with a laser diffraction particle size distribution analyzer (Shimadzu Corporation). As a control, an emulsion was similarly prepared using isolated soybean protein as a raw material, and the median diameter was measured. Table 2 shows the results.
- Test Example 2 Examination of molecular weight distribution Instead of isolated soy protein, soy peptide (Hinute AM, Fuji Oil Co., Ltd.), enzymatically isolated soy protein (Fuji Oil Co., Ltd.), or sample A of Patent Document 3 (hereinafter referred to as , referred to as the protein material of Patent Document 3), an emulsion was prepared in the same manner as in Test Example 1, and the median diameter was measured. Table 3 shows the results. In addition, the molecular weight distributions of the above Arg, the isolated soy protein, the enzyme-treated isolated soy protein, and the protein material of Patent Document 3 were measured according to the above method. The RT corresponding to the molecular weight of 20,000 Da was 38.4 minutes, the RT corresponding to 10,000 Da was 41.2 minutes, and the RT corresponding to 2,000 Da was 48.2 minutes. The results are shown in FIG. 1 and Table 4.
- the enzymatically isolated soy protein exhibits better emulsifying power than the isolated soy protein. It was expected that even better emulsifying power could be obtained by modification.
- Example 1 Preparation of denatured protein material To an aqueous solution of isolated soy protein (Fuji Oil Co., Ltd.), arginine was added as a denaturant to 0.5M. After heating this aqueous solution at 121° C. for 10 minutes, it was desalted, adjusted to pH 4.5 with hydrochloric acid, centrifuged at 10,000 G for 10 minutes, and the supernatant was recovered. The collected supernatant was desalted using an MW3500 dialysis tube, centrifuged again at 10,000 G for 10 minutes, and the supernatant was collected and freeze-dried to obtain denatured protein material A.
- isolated soy protein Frinine was added as a denaturant to 0.5M. After heating this aqueous solution at 121° C. for 10 minutes, it was desalted, adjusted to pH 4.5 with hydrochloric acid, centrifuged at 10,000 G for 10 minutes, and the supernatant was recovered. The collected supernatant was desalted using an
- Guanidine hydrochloride was added as a denaturing agent to an aqueous solution of soybean protein isolate (Fuji Oil Co., Ltd.) to a concentration of 4M. After heating this aqueous solution at 121° C. for 10 minutes, it was cooled, adjusted to pH 4.5 with hydrochloric acid, centrifuged at 10,000 G for 10 minutes, and the supernatant was recovered. The collected supernatant was desalted using an MW3500 dialysis tube, centrifuged again at 10,000 G for 10 minutes, and the supernatant was collected and freeze-dried to obtain denatured protein material B.
- Arginine was added as a denaturing agent to an aqueous solution of enzymatically separated soybean protein (Fuji Oil Co., Ltd.) at a concentration of 0.5M. After heating this aqueous solution at 121° C. for 10 minutes, it was desalted, adjusted to pH 4.5 with hydrochloric acid, centrifuged at 10,000 G for 10 minutes, and the supernatant was recovered. The collected supernatant was desalted using an MW3500 dialysis tube, centrifuged again at 10,000 G for 10 minutes, and the supernatant was collected and freeze-dried to obtain denatured protein material C.
- Urea was added as a denaturant to an aqueous solution of enzymatically separated soybean protein (Fuji Oil Co., Ltd.) at a concentration of 4M. After heating this aqueous solution at 121° C. for 10 minutes, it was desalted, adjusted to pH 4.5 with hydrochloric acid, centrifuged at 10,000 G for 10 minutes, and the supernatant was recovered. The collected supernatant was desalted using an MW3500 dialysis tube, centrifuged again at 10,000 G for 10 minutes, and the supernatant was collected and freeze-dried to obtain a denatured protein material D.
- Guanidine hydrochloride was added as a denaturing agent to an aqueous solution of enzymatically separated soybean protein (Fuji Oil Co., Ltd.) at a concentration of 4M. After heating this aqueous solution at 121° C. for 10 minutes, it was desalted using an MW3500 dialysis tube, centrifuged at 10,000 G for 10 minutes, and the supernatant was collected and freeze-dried to obtain denatured protein material E. Using the obtained denatured protein materials A to E, emulsions were prepared in the same manner as in Test Example 1, and the median diameter was measured. Table 5 shows the results. In addition, the molecular weight distributions of the denatured protein materials A to E were measured according to the method described above. The results are shown in FIG. 2 and Table 6. In addition, the protein content of these denatured protein materials was 80% by mass or more.
- denatured protein materials with specific molecular weight distributions exhibited improved emulsifying power.
- the protein material of Patent Document 3 showed emulsifying power at a crude protein amount of 1% or more, but the denatured protein material of the present invention showed good emulsifying power even from a crude protein amount of 0.5%.
- Denatured protein material A was dissolved in distilled water, and the pH was adjusted with NaOH to prepare a pH 7 10% by mass solution.
- the OD660nm of this solution measured at room temperature after standing overnight was 0.13.
- the viscosity of this solution at 60°C was 3.1 mPa ⁇ s.
- Example 2 Study on proteins other than soybeans Instead of isolated soybean proteins, isolated pea proteins, mung bean proteins, and broad bean proteins were subjected to denaturation and molecular weight distribution adjustment treatment to obtain denatured protein materials F, G, and H, respectively. rice field. As in Example 1, the median diameter of the emulsion and the molecular weight distribution of the protein material were measured. The results are shown in Tables 8 and 9. In addition, the protein content of these denatured protein materials was 80% by mass or more.
- denatured protein material with improved emulsifying power was obtained even when pea, mung bean, and fava bean proteins were used instead of soy protein.
- denatured protein materials did not become cloudy even when guanidine hydrochloride was added, but became cloudy when ammonium sulfate was added.
- a denatured protein material with a specific molecular weight distribution has improved emulsifying power compared to conventional protein materials.
- This denatured protein material can be used for foods, compositions, pharmaceutical compositions, and the like.
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Abstract
Description
この出願は、令和3年3月30日に日本国特許庁に出願された出願番号2021-056902号の優先権の利益を主張する。優先権基礎出願はその全体について、出典明示により本明細書の一部とする。
(1)下記a)~b)の全特徴を有する変性タンパク質素材:
a)分子量分布の測定結果で、2,000Da以上20,000Da未満の面積比率が45~90%、及び
b)粗タンパク質濃度0.1%の変性タンパク質素材の水溶液に250mM塩酸グアニジンを添加した場合に白濁せず、2M硫酸アンモニウムを添加した場合に白濁する;
(2)分子量分布の測定結果で、2,000Da未満の面積比率が45%以下である、(1)の変性タンパク質素材;
(3)分子量分布の測定結果で、10,000Da以上の面積比率が50%未満である、(1)の変性タンパク質素材;
(4)分子量分布の測定結果で、2,000Da未満の面積比率が45%以下であり、10,000Da以上の面積比率が50%未満である、(1)の変性タンパク質素材;
(5)変性タンパク質素材の、タンパク質含量が10質量%、pH7となるように調製した水溶液のOD660nmが0.5以下である、(1)の変性タンパク質素材;
(6)変性タンパク質素材の、タンパク質含量が10質量%、pH7となるように調製した水溶液のOD660nmが0.5以下である、(4)の変性タンパク質素材;
(7)動物性タンパク質を含まない、(1)の変性タンパク質素材;
(8)豆類由来のタンパク質である、(1)の変性タンパク質素材;
(9)豆類由来のタンパク質である、(4)の変性タンパク質素材;
(10)豆類由来のタンパク質である、(6)の変性タンパク質素材、
に関する。
a)分子量分布の測定結果で、2,000Da以上20,000Da未満の面積比率が45~90%、及び
b)粗タンパク質濃度0.1%の変性タンパク質素材の水溶液に250mM塩酸グアニジンを添加した場合に白濁せず、2M硫酸アンモニウムを添加した場合に白濁する。
本開示の変性タンパク質素材は、ゲルろ過によって分子量を測定した場合に、その分子量分布の面積比率は、2,000Da以上20,000Da未満が45~90%、例えば、50~85%、55~80%、55~75%、60~70%である。特許文献3に記載のタンパク質素材は、20,000Da以上の面積比率が55%を超えるものであり、この点で本開示の変性タンパク質素材と異なるものである。また、ある実施形態において、2,000Da未満の面積比率は45%以下、例えば、40%以下、35%以下、30%以下、25%以下である。下限は特に限定されないが、例えば0%以上、1%以上、2%以上、5%以上、10%以上、15%以上が挙げられる。また、他の実施形態において、10,000Da以上の面積比率は50%未満、例えば、5~45%、10~40%、15~35%である。さらに、他の実施形態において、20,000Da以上の面積比率は55%未満、例えば50%以下、40%以下、30%以下、25%以下、20%以下、15%以下である。
本開示の変性タンパク質素材は、水溶液に塩酸グアニジンを添加しても白濁しない。これは、タンパク質が十分に変性していることを示す指標であり、このことが、本開示のタンパク質素材が変性タンパク質素材と称される所以である。例えば、分離大豆タンパク質や、カゼインナトリウムなどの変性していないタンパク質に塩酸グアニジンを添加すると、白濁を生じる。本明細書において、塩酸グアニジンを添加して白濁しないことは、粗タンパク質濃度0.1%、塩酸グアニジン250mM水溶液において、目視で白濁がないこと、又は水溶液のOD660nmが0.3未満、例えば0.2以下、0.1以下、0であること、により確認できる。また、本開示の変性タンパク質素材は、水溶液に硫酸アンモニウムを添加すると白濁する。これは、タンパク質がある程度の重合度を有し、ジペプチド、トリペプチドのように過度に分解されたペプチドではないことを示す指標である。本明細書において、硫酸アンモニウムを添加して白濁することは、粗タンパク質濃度0.1%、硫酸アンモニウム2M水溶液において、目視で白濁が認められること、又は水溶液のOD660nmが0.3以上、例えば0.4以上、0.5以上であること、により確認できる。なお、塩酸グアニジン添加及び硫酸アンモニウム添加の手順は、後述する方法に基づくものとする。
より具体的な実施形態において、本開示の変性タンパク質素材は固形分中のタンパク質含量が40質量%以上であることが好ましく、例えば、50質量%以上、60質量%以上、70質量%以上、80質量%以上、85質量%以上、又は90質量%以上であることが好ましい。上記範囲に含まれる変性タンパク質素材の原料としては、分離タンパク質が好ましく、例えば大豆由来のタンパク質素材から調製する場合、分離大豆タンパク質などが挙げられる。豆乳レベルのタンパク質含量が低いものから調製した場合、タンパク質を高度に含有する乳化食品を製造するために多量に変性タンパク質素材を配合する必要が生じ、素材としての汎用性を損なう場合がある。
より具体的な実施形態において、本開示の変性タンパク質素材溶液の粘度を一定条件で測定したときに、低粘度であることが好ましく、具体的にはタンパク質含量が10質量%の水溶液の粘度が60℃で50mPa・s以下、例えば40mPa・s以下、35mPa・s以下、30mPa・s以下、20mPa・s以下、15mPa・s以下、10mPa・s以下、5mPa・s以下、が好ましい。また、粘度の下限は特に限定されないが、例えば0.1mPa・s以上、0.5mPa・s以上、1mPa・s以上等が挙げられる。なお、粘度は後述する方法により測定する。
より具体的な実施形態において、本開示の変性タンパク質素材は、室温での水への溶解度が20質量%以上、例えば25質量%以上である。溶解度の上限は特に限定されないが、例えば55質量%以下、50質量%以下、45質量%以下、40質量%以下、35質量%以下が挙げられる。
より具体的な実施形態において、本開示の変性タンパク質素材の水溶液は、好ましくは濁りが少なく、より好ましくは透明である。より具体的には、本開示の変性タンパク質素材の10%水溶液(pH7)を調製し、一晩静置後の室温でのOD660nmの値が、好ましくは0.5以下、例えば0.3以下、0.2以下、0.1以下、0である。
より具体的な実施形態において、本開示の変性タンパク質素材を含む乳化物のメディアン径は、4μm以下、例えば3μm以下、2μm以下、1μm以下である。より具体的には、粗タンパク質量1%以上、例えば0.5%以上、0.1%以上、0.05%以上で本開示の変性タンパク質素材を含む乳化物で上記のメディアン径を示す。乳化物の調製及びメディアン径の測定は、後述する方法に基づくものとする。
本開示の変性タンパク質素材は、タンパク質の変性と、分子量分布の調整を組み合わせることにより得られ得る。タンパク質を変性させる処理の例として、pH調整処理(例えば、酸処理、アルカリ処理)、変性剤処理、加熱処理、冷却処理、高圧処理、有機溶媒処理、ミネラル添加処理、超臨界処理、超音波処理、電気分解処理及びこれらの組み合わせ等が挙げられる。分子量分布を調整する処理の例として、酵素処理、ろ過、ゲルろ過、クロマトグラフィー、遠心分離、電気泳動、透析及びこれらの組み合わせ等が挙げられる。タンパク質を変性させる処理と、分子量分布を調整する処理の順序及び回数は特に限定されず、タンパク質を変性させる処理を行ってから分子量分布を調整する処理を行ってもよいし、分子量分布を調整する処理を行ってからタンパク質を変性させる処理を行ってもよいし、両処理を同時に行ってもよい。また、例えば2回以上の分子量分布を調整する処理の間にタンパク質を変性する処理を行う、2回以上のタンパク質を変性する処理の間に分子量分布を調整する処理を行う、各々複数回の処理を任意の順に行う、等も可能である。なお、タンパク質を変性させる処理によって所望の分子量分布が得られる場合は、分子量分布の調整のための処理を行わなくてもよい。これらの処理を組み合わせて、複数回行う際、原料から全ての処理を連続で行ってもよいし、時間をおいてから行ってもよい。例えば、ある処理を経た市販品を原料として他の処理を行ってもよい。本明細書において、このような処理を便宜上「変性・分子量分布調整処理」と称する。なお、上記特性を満たす限り、変性・分子量分布調整処理を経た変性タンパク質素材と、変性・分子量分布調整処理を経ていないタンパク質を混合して、特定の変性タンパク質素材としてもよい。この場合、両者の比率(変性・分子量分布調整処理を経たタンパク質素材:変性・分子量分布調整処理を経ていないタンパク質)は上記特性を満たす範囲で適宜調整可能であるが、質量比で例えば1:99~99:1、例えば50:50~95:5、75:25~90:10等が挙げられる。ある実施形態では、本開示の変性タンパク質素材は、変性・分子量分布調整処理を経た植物性タンパク質素材からなる。
本明細書において、変性タンパク質素材に関する成分や物性の測定は、以下の方法に準ずる。
ケルダール法により測定する。具体的には、105℃で12時間乾燥したタンパク質素材質量に対して、ケルダール法により測定した窒素の質量を、乾燥物中のタンパク質含量として「質量%」で表す。なお、窒素換算係数は6.25とする。基本的に、小数点以下第2桁の数値を四捨五入して求められる。
溶離液でタンパク質素材を0.1質量%濃度に調整し、0.2μmフィルターでろ過したものを試料液とする。2種のカラム直列接続によってゲルろ過システムを組み、はじめに分子量マーカーとなる既知のタンパク質等(表1)をチャージし、分子量と保持時間の関係において検量線を求める。次に試料液をチャージし、各分子量画分の含有量比率%を全体の吸光度のチャート面積に対する、特定の分子量範囲(時間範囲)の面積の割合によって求める(1stカラム:「TSK gel G3000SWXL」(SIGMA-ALDRICH社)、2ndカラム:「TSK gel G2000SWXL」(SIGMA-ALDRICH社)、溶離液:1%SDS+1.17%NaCl+50mMリン酸バッファー(pH7.0)、23℃、流速:0.4ml/分、検出:UV220nm)。基本的に、小数点以下第2桁の数値を四捨五入して求められる。
粗タンパク質濃度が0.2%のタンパク質素材の水溶液を調製する。水溶液調製時に白濁した場合は、1ないし10%程度の水溶液を調製後遠心分離し、上清を回収し、粗タンパク質濃度0.2%となるよう希釈して試料溶液とする。これに塩酸グアニジン溶液を等量添加して粗タンパク質濃度0.1%、塩酸グアニジン濃度250mMの溶液を調製し、一晩冷蔵庫で静置する。目視で白濁の有無を確認する。あわせて、10mmガラスセルを用いて、波長660nmで濁度を測定する。
粗タンパク質濃度が0.2%のタンパク質素材の水溶液を調製する。水溶液調製時に白濁した場合は、1ないし10%程度の水溶液を調製後遠心分離し、上清を回収し、粗タンパク質濃度0.2%となるよう希釈して試料溶液とする。これに硫酸アンモニウム溶液を等量添加して粗タンパク質濃度0.1%、硫酸アンモニウム濃度2Mの溶液を調製し、一晩冷蔵庫で静置する。目視で白濁の有無を確認する。あわせて、10mmガラスセルを用いて、波長660nmで濁度を測定する。
タンパク質素材の粘度は、タンパク質含量が10質量%となるように該タンパク質素材の水溶液を調製し、60℃にてB型粘度計(望ましくはBrookfield社)でローターは「#LV-1」を使用し、100rpmで1分後に示された測定値として求められる。「#LV-1」で測定不能な場合は順次ローターを「#LV-2」、「#LV-3」、「#LV-4」、「#LV-5」に代えて使用する。「#LV-1」/100rpmで低粘度により測定不能の場合は「下限」とし、「#LV-5」/100rpmで高粘度により測定不能な場合は「上限」とする。
メディアン径は、レーザ回折式粒度分布測定装置(望ましくは株式会社島津製作所)で測定する。変性タンパク質素材、油脂、水を混合し、粗タンパク質量1%、0.5%、0.1%、0.05%、油分20%の乳化物を調製して試料とする。基本的に、小数点以下第2桁の数値、数値が低い場合は有効数字を2桁として次の桁の数値、を四捨五入して求められる。
分離大豆タンパク質(不二製油株式会社)水溶液に、変性剤としてアルギニンを0.5Mとなるように添加した。その後、この水溶液を121℃10分間加熱した後、MW3500透析チューブを用いて変性剤を除去した後、フリーズドライして粉末状のタンパク質素材(Argと称する)を得た。Arg、MCT64(中鎖脂肪酸油脂、不二製油株式会社)、水を混合して、油分20%、粗タンパク質濃度1%、0.5%、0.1%、0.05%となるように混合し、超音波処理により乳化物を調製した。調製した乳化物を冷蔵保管した後、メディアン径をレーザ回折式粒度分布測定装置(株式会社島津製作所)で測定した。対照として、原料の分離大豆タンパク質を使用して同様に乳化物を調製し、メディアン径を測定した。結果を表2に示す。
分離大豆タンパク質の代わりに、大豆ペプチド(ハイニュートAM、不二製油株式会社)、酵素分解分離大豆タンパク質(不二製油株式会社)又は特許文献3のサンプルA(以下、特許文献3のタンパク質素材と称する)を用いて、試験例1と同様に乳化物を調製し、メディアン径を測定した。結果を表3に示す。また、上記Arg、分離大豆タンパク質、酵素処理分離大豆タンパク質、特許文献3のタンパク質素材の分子量分布を、上記方法に従って測定した。なお、分子量20,000Daに対応するRTは38.4分、10,000Daに対応するRTは41.2分、2,000Daに対応するRTは48.2分であった。結果を図1、表4に示す。
分離大豆タンパク質(不二製油株式会社)水溶液に、変性剤としてアルギニンを0.5Mとなるように添加した。この水溶液を121℃10分間加熱した後、脱塩し、塩酸でpH4.5に調整し、10,000G、10分間遠心分離し、上清を回収した。回収した上清をMW3500透析チューブを用いて脱塩し、再度10,000G、10分間遠心分離し、上清を回収して、フリーズドライに供し、変性タンパク質素材Aを得た。
分離大豆タンパク質(不二製油株式会社)水溶液に、変性剤として塩酸グアニジンを4Mとなるように添加した。この水溶液を121℃10分間加熱した後、冷却し、塩酸でpH4.5に調整し、10,000G、10分間遠心分離し、上清を回収した。回収した上清をMW3500透析チューブを用いて脱塩し、再度10,000G、10分間遠心分離し、上清を回収して、フリーズドライに供し、変性タンパク質素材Bを得た。
酵素分解分離大豆タンパク質(不二製油株式会社)水溶液に、変性剤としてアルギニンを0.5Mとなるように添加した。この水溶液を121℃10分間加熱した後、脱塩し、塩酸でpH4.5に調整し、10,000G、10分間遠心分離し、上清を回収した。回収した上清をMW3500透析チューブを用いて脱塩し、再度10,000G、10分間遠心分離し、上清を回収して、フリーズドライに供し、変性タンパク質素材Cを得た。
酵素分解分離大豆タンパク質(不二製油株式会社)水溶液に、変性剤として尿素を4Mとなるように添加した。この水溶液を121℃10分間加熱した後、脱塩し、塩酸でpH4.5に調整し、10,000G、10分間遠心分離し、上清を回収した。回収した上清をMW3500透析チューブを用いて脱塩し、再度10,000G、10分間遠心分離し、上清を回収して、フリーズドライに供し、変性タンパク質素材Dを得た。
酵素分解分離大豆タンパク質(不二製油株式会社)水溶液に、変性剤として塩酸グアニジンを4Mとなるように添加した。この水溶液を121℃10分間加熱した後、MW3500透析チューブを用いて脱塩し、10,000G、10分間遠心分離し、上清を回収して、フリーズドライに供し、変性タンパク質素材Eを得た。
得られた変性タンパク質素材A~Eを用いて、試験例1と同様に乳化物を調製し、メディアン径を測定した。結果を表5に示す。また、変性タンパク質素材A~Eの分子量分布を、上記方法に従って測定した。結果を図2、表6に示す。また、これら変性タンパク質素材のタンパク質含量は、どれも80質量%以上であった。
変性タンパク質素材A~E、大豆ペプチド、酵素分解分離大豆タンパク質、分離大豆タンパク質に対して、上記の方法に基づき塩酸グアニジン及び硫酸アンモニウムの添加を行った。結果を表7に示す。
分離大豆タンパク質の代わりに、分離エンドウ豆タンパク質、リョクトウタンパク質、ソラマメタンパク質を変性・分子量分布調整処理に供して、それぞれ変性タンパク質素材F、G、Hを得た。実施例1と同様に、乳化物のメディアン径及びタンパク質素材の分子量分布を測定した。結果を表8、9に示す。また、これら変性タンパク質素材のタンパク質含量は、どれも80質量%以上であった。
Claims (10)
- 下記a)~b)の全特徴を有する変性タンパク質素材:
a)分子量分布の測定結果で、2,000Da以上20,000Da未満の面積比率が45~90%、及び
b)粗タンパク質濃度0.1%の変性タンパク質素材の水溶液に250mM塩酸グアニジンを添加した場合に白濁せず、2M硫酸アンモニウムを添加した場合に白濁する。 - 分子量分布の測定結果で、2,000Da未満の面積比率が45%以下である、請求項1に記載の変性タンパク質素材。
- 分子量分布の測定結果で、10,000Da以上の面積比率が50%未満である、請求項1に記載の変性タンパク質素材。
- 分子量分布の測定結果で、2,000Da未満の面積比率が45%以下であり、10,000Da以上の面積比率が50%未満である、請求項1に記載の変性タンパク質素材。
- 変性タンパク質素材の、タンパク質含量が10質量%、pH7となるように調製した水溶液のOD660nmが0.5以下である、請求項1に記載の変性タンパク質素材。
- 変性タンパク質素材の、タンパク質含量が10質量%、pH7となるように調製した水溶液のOD660nmが0.5以下である、請求項4に記載の変性タンパク質素材。
- 動物性タンパク質を含まない、請求項1に記載の変性タンパク質素材。
- 豆類由来のタンパク質である、請求項1に記載の変性タンパク質素材。
- 豆類由来のタンパク質である、請求項4に記載の変性タンパク質素材。
- 豆類由来のタンパク質である、請求項6に記載の変性タンパク質素材。
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