WO2024172143A1 - 改質された蛋白質含有食品の製造方法 - Google Patents

改質された蛋白質含有食品の製造方法 Download PDF

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Publication number
WO2024172143A1
WO2024172143A1 PCT/JP2024/005400 JP2024005400W WO2024172143A1 WO 2024172143 A1 WO2024172143 A1 WO 2024172143A1 JP 2024005400 W JP2024005400 W JP 2024005400W WO 2024172143 A1 WO2024172143 A1 WO 2024172143A1
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WIPO (PCT)
Prior art keywords
sample
protein
pld
foods
added
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PCT/JP2024/005400
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English (en)
French (fr)
Japanese (ja)
Inventor
孝彰 安部
哲郎 堀
卓也 大貫
藤村 祐子 曽我
夏樹 宮崎
智子 金子
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Ajinomoto Co Inc
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Ajinomoto Co Inc
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Priority to JP2025501225A priority Critical patent/JPWO2024172143A1/ja
Priority to EP24756983.3A priority patent/EP4666864A1/en
Publication of WO2024172143A1 publication Critical patent/WO2024172143A1/ja
Priority to US19/299,907 priority patent/US20250366492A1/en
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • 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
    • A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal 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; PREPARATION THEREOF
    • A23C9/00—Milk preparations; Milk powder or milk powder preparations
    • A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
    • A23C9/1203—Addition of, or treatment with, enzymes or microorganisms other than lactobacteriaceae
    • A23C9/1216—Other enzymes
    • 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
    • A23J3/22—Working-up of proteins for foodstuffs by texturising
    • 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
    • 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
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
    • A23L13/70—Tenderised or flavoured meat pieces; Macerating or marinating solutions specially adapted therefor
    • A23L13/72—Tenderised or flavoured meat pieces; Macerating or marinating solutions specially adapted therefor using additives, e.g. by injection of solutions
    • A23L13/74—Tenderised or flavoured meat pieces; Macerating or marinating solutions specially adapted therefor using additives, e.g. by injection of solutions using microorganisms or enzymes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • 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
    • A23L33/145—Extracts
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • 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
    • A23L33/16—Inorganic salts, minerals or trace elements
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • 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
    • A23L33/175—Amino acids
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y301/00—Hydrolases acting on ester bonds (3.1)
    • C12Y301/04—Phosphoric diester hydrolases (3.1.4)
    • C12Y301/04004—Phospholipase D (3.1.4.4)

Definitions

  • the present invention relates to a method for producing modified protein-containing foods, an enzyme preparation for modifying protein-containing foods, a pickling solution for meat processing to modify the proteins in processed meat foods, and a method for modifying protein-containing foods.
  • Patent Document 1 discloses a method for producing a meat product without the addition of egg white-derived ingredients, characterized by using transglutaminase and carrageenan.
  • Patent Document 2 aims to provide a texture-improving composition that can impart a good egg white-like texture when used as a food ingredient, and discloses a texture-improving composition that contains swelling-inhibited starch and wheat protein.
  • Patent Document 3 discloses a method for producing processed livestock foods such as sausages and hams that can be produced using only vegetable raw materials without adding egg white, and the method uses transglutaminase. None of these documents describes the use of phospholipase D to improve the texture of protein-containing foods.
  • the object of the present invention is to provide a method for producing protein-containing foods (particularly foods containing a relatively large amount of protein ingredients) with improved unpleasant texture.
  • the inventors have conducted intensive research to solve the above problems and have found that adding a protein raw material and phospholipase D (sometimes referred to as "PLD” in this specification) during the manufacturing process of processed foods and the like can impart a smooth texture without imparting unpleasant textures such as “roughness” or “grittyness” derived from proteins.
  • PLD protein raw material and phospholipase D
  • the present invention is as follows.
  • a method for producing a modified protein-containing food comprising treating a protein-containing food raw material with phospholipase D.
  • the food raw material contains at least one selected from the group consisting of the following (A) to (I): (A) an alkali salt; (B) a calcium salt or calcium oxide; (C) a magnesium salt or magnesium oxide; (D) a reducing agent; (E) a metal ion; (F) a nonpolar amino acid or a nonpolar amino acid salt; (G) an uncharged amino acid or an uncharged amino acid salt; (H) a basic amino acid or a basic amino acid salt; (I) an acidic amino acid or an acidic amino acid salt.
  • [12] The method according to any one of [1] to [11] above, further comprising treating with an enzyme that contributes to the formation of a crosslinked structure.
  • [12-1] The method for producing the above-mentioned [12], wherein the enzyme that contributes to the formation of the crosslinked structure is transglutaminase.
  • [12-2] The method according to the above [12], wherein the enzyme contributing to the formation of the crosslinked structure is ascorbic acid oxidase, and the food raw material contains L-ascorbic acid or a similar compound.
  • [12-3] The production method according to the above [12], wherein the enzyme that contributes to the formation of the crosslinked structure is glucose oxidase, and the food raw material contains glucose.
  • a method for modifying a protein-containing food comprising treating a protein-containing food raw material with phospholipase D.
  • the method for modifying food according to the above [20], wherein the enzyme contributing to the formation of the crosslinked structure is ascorbic acid oxidase, and the food raw material contains L-ascorbic acid or the like.
  • [20-3] The method for modifying food according to the above [20], wherein the enzyme that contributes to the formation of a crosslinked structure is glucose oxidase, and the food raw material contains glucose.
  • [21] The method for modifying the protein-containing food described in [19] or [20] above, wherein the protein-containing food is selected from the group consisting of processed meat foods, processed rice foods, processed soybean foods, processed wheat foods, processed egg foods, processed dairy foods, processed seafood foods, and plant-based foods.
  • the present invention it is possible to provide a protein-containing food in which the unpleasant texture derived from protein has been improved. According to the present invention, it is possible to provide foods in which the unpleasant texture derived from proteins is suppressed even when a relatively large amount of protein raw material is added.
  • the present invention is applicable to a wide range of protein-containing foods, such as processed meat products, processed seafood products, and plant-based foods.
  • FIG. 1 shows a sample preparation flow in Test Example 1.
  • FIG. 2 shows a sample preparation flow in Test Example 2.
  • FIG. 3 shows a sample preparation flow in Test Example 3.
  • FIG. 4 shows a sample preparation flow in Test Example 4.
  • FIG. 5 shows a sample preparation flow in Test Example 5.
  • FIG. 6 shows a sample preparation flow in Test Example 6.
  • FIG. 7 shows a sample preparation flow in Test Example 7.
  • FIG. 8 shows a sample preparation flow in Test Example 8.
  • FIG. 9 shows a sample preparation flow in Test Example 9.
  • FIG. 10 shows the sample preparation flow in Test Examples 12, 13, 14, 15, 16, and 19.
  • FIG. 11 shows a sample preparation flow in Test Example 17.
  • FIG. 12 shows a sample preparation flow in Test Example 18.
  • FIG. 13 shows a sample preparation flow in Test Example 20.
  • FIG. 14 shows the sample preparation flow in Test Examples 21 and 22.
  • FIG. 15 shows a sample preparation flow in Test Example 23.
  • FIG. 16 shows a sample preparation flow in Test Example 24.
  • FIG. 17 shows a sample preparation flow in Test Example 25.
  • FIG. 18 shows a sample preparation flow in Test Example 26.
  • FIG. 19 shows a sample preparation flow in Test Example 27.
  • FIG. 20 shows a sample preparation flow in Test Example 28.
  • FIG. 21 shows a sample preparation flow in Test Example 29.
  • FIG. 22-1 shows the sample preparation flow in Test Examples 30, 31, and 32.
  • FIG. 22-2 shows the sensory evaluation method in Test Examples 30, 31, and 32.
  • the present invention relates to a method for producing a modified protein-containing food.
  • the method for producing the modified protein-containing food of the present invention (hereinafter also simply referred to as the production method of the present invention) comprises treating a protein-containing food raw material with phospholipase D.
  • examples of protein-containing foods include processed foods produced from food ingredients containing protein (hereinafter, simply referred to as "food ingredients").
  • food ingredients containing protein include meats such as beef, pork, and chicken; fish such as Alaska pollock, hairtail, and threadfin bream; seafood (marine products) such as shellfish, shrimp, crab, octopus, and squid; grains such as rice and wheat; milk, eggs, and proteins derived from plants or animals (e.g., vegetable proteins such as soy protein, wheat protein, oat protein, pea protein, broad bean protein, mung bean protein, rice protein, chickpea protein, rapeseed protein, corn powder, oatmeal powder, almond protein, peanut powder, spirulina, soy milk, oat milk, and coconut milk; and animal proteins such as egg white, egg white (powder), milk protein, skim milk powder, whey powder, casein or a salt thereof (e.g., sodium caseinate), cricket powder (Cricket
  • protein-containing foods include processed meat foods such as ham, sausage, hamburger steak, and fried chicken; processed egg foods such as omelets; processed rice foods such as cooked rice, rice flour bread, and rice vermicelli; processed soybean foods such as tofu; processed wheat foods such as bread, noodles (e.g., Chinese noodles, udon), sweets (snacks), gyoza (dumplings) and burrito (dumplings); processed egg foods such as mayonnaise; processed dairy foods such as ice cream, yogurt, and cheese; processed seafood foods such as chikuwa and kamaboko; plant-based foods in which the animal protein of the above foods is replaced with plant protein (plant-based (PB) cheese (also called cheese analogue), plant-based yogurt, plant-based eggs, plant-based snacks (formed, bars)); and semi-solid liquid foods of the above protein-containing foods.
  • PB plant-based
  • cheese also called cheese analogue
  • plant-based yogurt plant-based eggs
  • plant-based snacks formed, bars
  • processed seafood foods refers to foods made from seafood such as fish, shellfish, shrimp, crab, octopus, and squid.
  • the manner in which the protein-containing foods are provided is not particularly limited. That is, the protein-containing foods may be provided in any manner, such as raw foods, heated products, frozen products, aseptically packaged products, retort products, dried products, canned products, and the like.
  • the present invention is particularly advantageous for use with solid or semi-solid protein-containing foods that require not only smoothness but also a suitable degree of hardness and elasticity when consumed.
  • a solid protein-containing food refers to a food that contains protein and is in a solid state (in other words, a non-fluid state, a gelled state, and one that maintains its shape against gravity).
  • protein-containing solid foods in the present invention include ham, sausage, hamburger steak, fried chicken, cooked rice, rice flour bread, rice vermicelli, bread, noodles (e.g., Chinese noodles, udon), sweets, gyoza (dumplings), burrito (dumplings), cheese, chikuwa (fish cake), kamaboko (fish paste), and plant-based foods in which the animal protein in these foods is replaced with plant protein.
  • a semi-solid protein-containing food refers to a food that contains protein and has the properties of both liquid and solid, and is in a semi-fluid state that is closer to solid than liquid.
  • protein-containing semi-solid foods in the present invention include tofu, mayonnaise, ice cream, yogurt, semi-solid liquid foods, and plant-based foods in which the animal protein in these foods is replaced with vegetable protein.
  • a vegetable or animal-derived protein e.g., vegetable protein such as soy protein or wheat protein; animal protein such as egg white, milk protein, casein or a salt thereof (e.g., sodium caseinate), cricket powder, etc.
  • a vegetable or animal-derived protein e.g., vegetable protein such as soy protein or wheat protein; animal protein such as egg white, milk protein, casein or a salt thereof (e.g., sodium caseinate), cricket powder, etc.
  • Phospholipase is an enzyme that has the activity of hydrolyzing phospholipids.
  • activity units of phospholipase D are measured and defined as follows: 0.1 mL of enzyme solution is mixed with 0.9 mL of substrate solution containing phosphatidylcholine, and reacted at 37° C. for 30 minutes. After the reaction is stopped, 50 ⁇ L of the reaction solution is added to 1 mL of color-developing solution containing choline oxidase, peroxidase, etc., and reacted for 5 minutes. After the reaction is stopped, the amount of pigment produced from choline is measured. The amount of enzyme that liberates 1 ⁇ mole of choline per minute at 37° C. using phosphatidylcholine as a substrate is defined as 1 U (unit).
  • the amount of phospholipase D added is such that the enzyme activity per 1 g of protein is preferably 0.000000065 U or more, more preferably 0.00000065 U or more, and even more preferably 0.000065 U or more.
  • the amount of phospholipase D added is such that the enzyme activity per gram of protein is preferably 30,000 U or less, more preferably 15,000 U or less, and even more preferably 6,494 or less.
  • the amount of phospholipase D added is preferably 0.000000065 to 300000 U, more preferably 0.00000065 to 150000 U, and even more preferably 0.000065 to 6494 U in terms of enzyme activity per 1 g of protein.
  • the amount of phospholipase D added is preferably 0.1 U or more, more preferably 1.2 to 10,000.0 U, and even more preferably 12.0 to 5,000.0 U in terms of enzyme activity per gram of protein.
  • the action time (reaction time) of phospholipase D is not particularly limited as long as the enzyme can act on the substrate phospholipid, but examples of the time include 0 minutes or more, 1 minute or more, 3 minutes or more, 5 minutes or more, 10 minutes or more, 20 minutes or more, and 30 minutes or more. Examples of the time include 168 hours or less, 72 hours or less, 48 hours or less, 24 hours or less, 12 hours or less, 6 hours or less, 3 hours or less, 2 hours or less, and 1 hour or less.
  • a practical action time is preferably 0 to 148 hours, and more preferably 30 minutes to 148 hours.
  • the action temperature is also not particularly limited as long as the enzyme maintains its activity, but a practical temperature of 0 to 60°C is preferable.
  • the enzyme reaction can be terminated by heating at, for example, 70 to 75°C for 5 to 10 minutes.
  • the enzyme that contributes to the formation of a crosslinked structure is an enzyme that has the activity of acting directly or indirectly on a protein to form a cross-linked structure in the protein.
  • examples of the enzyme that contributes to the formation of a crosslinked structure include transglutaminase, ascorbic acid oxidase, and glucose oxidase.
  • the food raw material to which the enzyme is added contains L-ascorbic acids (meaning ascorbic acid, ascorbate salts, or those with a modified ascorbic acid skeleton, examples of which include salts with alkali metals or alkaline earth metals (e.g., sodium ascorbate, calcium ascorbate, etc.), the provitamin ascorbic acid 2-glucoside, ascorbic acid esters (e.g., ascorbyl palmitate, ascorbyl stearate, etc.), and materials rich in ascorbic acid, with ascorbic acid and sodium ascorbate being preferred.
  • L-ascorbic acids meaning ascorbic acid, ascorbate salts, or those with a modified ascorbic acid skeleton, examples of which include salts with alkali metals or alkaline earth metals (e.g., sodium ascorbate, calcium ascorbate, etc.), the provitamin ascorbic acid 2-glucoside, ascorbic acid esters (e.g.,
  • the amount of L-ascorbic acids in the food raw material to which the enzyme is added is, for example, 0.000000000001 to 50.0 wt%, preferably 0.00000000001 to 30.0 wt%, more preferably 0.0000000001 to 10.0 wt%, and even more preferably 0.000000001 to 6.0 wt%, per gram of the protein to which the enzyme is added.
  • the amount of L-ascorbic acids in the food raw material to which the enzyme is added is, for example, 0.1 to 99 wt %, preferably 1 to 95 wt %, more preferably 5 to 90 wt %, and even more preferably 10 to 80 wt %, calculated as ascorbic acid, relative to the agent of the present invention.
  • the food raw material to which the enzyme is added contains glucose as a substrate.
  • the amount of glucose in the food raw material to which the enzyme is added is 0.0000000001 to 10.0 wt%, preferably 0.000000001 to 5.0 wt%, more preferably 0.00000001 to 1.0 wt%, and even more preferably 0.0000001 to 0.1 wt%, per 1 g of the protein to which the enzyme is added.
  • the amount of glucose in the food raw material to which the enzyme is added is, for example, 0.1 to 99 wt %, preferably 0.2 to 95 wt %, more preferably 0.5 to 90 wt %, and even more preferably 1 to 80 wt %, relative to the agent of the present invention.
  • the order of addition may be any order, and they may be added all at the same time or in sequence with a time lag; however, from the standpoint of simplicity, it is preferable to add all at the same time.
  • the reaction time, reaction temperature, and method of terminating the enzyme reaction are the same as those for phospholipase D described above.
  • the enzymes to be reacted with the food raw materials include the following (I) to (VII).
  • (I) to (VII) are collectively referred to as "the enzymes in the present invention.
  • (I) Phospholipase D Phospholipase D and transglutaminase
  • III Phospholipase D and ascorbate oxidase
  • IV Phospholipase D, transglutaminase and ascorbate oxidase
  • V Phospholipase D and glucose oxidase
  • V Phospholipase D and glucose oxidase
  • the transglutaminase used in the present invention is an enzyme that has the activity of catalyzing an acyl transfer reaction in which a glutamine residue in a protein or peptide is used as a donor and a lysine residue is used as an acceptor, and transglutaminase of various origins is known, such as those derived from mammals, fish, and microorganisms.
  • the transglutaminase used in the present invention is not particularly limited in origin as long as it has the above-mentioned activity, and transglutaminase of any origin can be used, and recombinant enzymes can also be used.
  • the transglutaminase used in the present invention may be a commercially available product, and as a specific example, microbial transglutaminase commercially available from Ajinomoto Co., Inc. under the product name "Activa" TG can be used alone or in combination.
  • the enzyme activity of transglutaminase is measured by reacting transglutaminase in a reaction system with benzyloxycarbonyl-L-glutamylglycine and hydroxylamine as substrates in a Tris buffer solution at 37°C and pH 6.0, forming an iron complex with the hydroxamic acid produced in the presence of trichloroacetic acid, measuring the absorbance at 525 nm, and determining the amount of hydroxamic acid using a calibration curve.
  • One unit (1U) of enzyme is defined as the amount of enzyme that produces 1 ⁇ mole of hydroxamic acid per minute (see JP 64-27471 A).
  • the amount of transglutaminase added is, for example, 0.01 to 25.6 U, preferably 0.06 to 12.8 U, more preferably 0.3 to 6.4 U, and even more preferably 0.6 to 3.2 U in terms of enzyme activity per 1 g of protein. Furthermore, when transglutaminase is used in the production method of the present invention, the amount of transglutaminase added is, for example, 0.01 to 22.0 U, preferably 0.1 to 11.0 U, more preferably 0.2 to 5.5 U, and even more preferably 0.5 to 3.5 U in terms of enzyme activity per 1 g of protein.
  • the ascorbic acid oxidase (enzyme number EC1.10.3.3) used in the present invention is one of the ascorbic acid/aldaric acid metabolic enzymes, and is an oxidoreductase that catalyzes a chemical reaction that produces dehydroascorbic acid and water using ascorbic acid and oxygen as substrates.
  • ascorbic acid oxidase derived from Cucurbitaceae plants such as pumpkin, cucumber, and zucchini has been widely used industrially, but the ascorbic acid oxidase used in the present invention is not particularly limited in origin as long as it has the above-mentioned activity, and may be derived from, for example, a plant, a microorganism, or an animal.
  • the ascorbic acid oxidase used in the present invention may be a recombinant enzyme.
  • the method for producing the ascorbic acid oxidase used in the present invention is not particularly limited, and ascorbic acid oxidase produced by a method known per se or a method equivalent thereto may be used.
  • Ascorbic acid oxidase a commercially available product may be used.
  • the ascorbic acid oxidase may be used alone or in combination of two or more kinds.
  • the activity unit of ascorbic acid oxidase is defined as 1 U (unit) as the amount of enzyme that oxidizes 1 ⁇ mol of ascorbic acid per minute under conditions of 30° C. and pH 5.6.
  • the activity of ascorbic acid oxidase is measured by the following procedures (1) to (3). (1) Place 1 mL of 0.001 mol/L ascorbic acid solution and 1 mL of 0.01 mol/L disodium hydrogen phosphate in a test tube and preheat for 5 minutes in a thermostatic water bath at 30°C. Add 0.2 mL of the diluted test enzyme solution to this mixture (pH 5.6) and immediately stir to react.
  • the absorbance (Abs2) of this solution at a wavelength of 245 nm is measured.
  • the amount of ascorbic acid oxidase to be added is, for example, 0.00000012 to 12000000000000 U, preferably 0.0000012 to 1200000000000 U, more preferably 0.000012 to 120000000000 U, and even more preferably 0.00012 to 120000000000 U in terms of enzyme activity per 1 g of the content of the substrate of the enzyme (converted into L-ascorbic acid).
  • the amount of ascorbic acid oxidase to be added is, for example, 0.5 to 500 U, preferably 1 to 350 U, more preferably 3 to 200 U, and even more preferably 5 to 100 U in terms of enzyme activity per 1 g of the content of the substrate of the enzyme (converted into L-ascorbic acid).
  • the glucose oxidase (EC 1.1.3.4) used in the present invention is an enzyme that catalyzes a reaction in which glucose and oxygen are used as substrates to produce gluconolactone (gluconolactone is non-enzymatically hydrolyzed to gluconic acid) and hydrogen peroxide.
  • the hydrogen peroxide produced by this reaction oxidizes the SH groups in proteins, promoting the production of SS bonds (disulfide bonds) and forming cross-linked structures in proteins.
  • Glucose oxidases of various origins are known, including those derived from microorganisms such as koji mold and those derived from plants, and any of these glucose oxidases may be used, and there is no restriction on the origin.
  • glucose oxidase is the microbial glucose oxidase commercially available from Shin-Nihon Kagaku Kogyo Co., Ltd. under the product name "Sumiteam PGO.”
  • the activity unit of glucose oxidase is defined as 1 U (unit) as the amount of enzyme that oxidizes 1 ⁇ mol of glucose per minute at 37° C. and pH 7.0.
  • the activity of glucose oxidase can be exemplified by the following method. Glucose is used as a substrate, and hydrogen peroxide is generated by acting glucose oxidase in the presence of oxygen. A quinoneimine dye is generated by acting peroxidase on the generated hydrogen peroxide in the presence of aminoantipyrine and phenol. The generated quinoneimine dye is measured at a wavelength of 500 nm. Specifically, the method is as follows.
  • Glucose oxidase is stirred and dissolved in 0.1 mol/L phosphate buffer (adjusted to pH 7.0 with potassium dihydrogen phosphate and sodium hydroxide aqueous solution), and then diluted 50 times with 0.1 mol/L phosphate buffer to obtain a GO solution.
  • a phenol-containing buffer solution (Milli-Q, 1.36 g of potassium dihydrogen phosphate, 3 mL of 5% phenol test solution, and 3 mL of 5% Triton X-100 solution are mixed and adjusted to pH 7.0 with sodium hydroxide aqueous solution, 100 mL), 500 ⁇ L of a 10% glucose solution, 500 ⁇ L of a 0.01% peroxidase solution (PO "amano" 3 (1250 U ⁇ 250 U) is used), and 100 ⁇ L of a 0.4% 4-aminoantipyrine solution are added in order, mixed by inversion, and kept at 37 ⁇ 0.1 ° C. for 10 minutes.
  • a phenol-containing buffer solution (Milli-Q, 1.36 g of potassium dihydrogen phosphate, 3 mL of 5% phenol test solution, and 3 mL of 5% Triton X-100 solution are mixed and adjusted to pH 7.0 with sodium hydroxide aqueous solution, 100 mL)
  • GO activity value is measured from the increment (slope) between 120 seconds and 300 seconds.
  • the value measured by adding 0.1 mol/L phosphate buffer instead of the GO solution was used and subtracted from the value measured for the GO test group.
  • the amount of enzyme required to oxidize or reduce 1 ⁇ mol of substrate per minute is defined as 1 U (unit).
  • the amount of glucose oxidase to be added is, for example, 0.0000000022 to 215000000000 U, preferably 0.000000022 to 21500000000 U, more preferably 0.00000022 to 2150000000 U, and even more preferably 0.0000022 to 2150000000 U in terms of enzyme activity per 1 g of the substrate (glucose) of the enzyme.
  • the amount of glucose oxidase to be added is, for example, 0.01 to 10,000 U, preferably 0.1 to 5,000 U, more preferably 0.5 to 3,000 U, and even more preferably 1.0 to 2,000 U in terms of enzyme activity per 1 g of the substrate (glucose) of the enzyme.
  • the food raw material to which the enzyme is added preferably contains an auxiliary material selected from the following (A) to (N).
  • auxiliary materials may be contained alone or in combination of two or more.
  • an alkali salt e.g., sodium carbonate, trisodium phosphate, tripotassium phosphate, trisodium citrate
  • B calcium salts, calcium oxide (e.g., calcium chloride, calcined shell calcium, calcium lactate, calcium carbonate);
  • C magnesium salts, magnesium oxide (e.g., magnesium chloride, magnesium glutamate);
  • D a reducing agent (e.g., glutathione-containing yeast extract, cysteine-containing yeast extract),
  • metal ions e.g., iron-containing yeast, copper-containing yeast, manganese-containing yeast);
  • F nonpolar amino acids and nonpolar amino acid salts (e.g., glycine, cystine, alanine, valine, leucine, isoleucine, phenylalanine, proline, methionine);
  • G uncharged amino acids and uncharged amino acid salts (e.g., threonine, serine, glutamine,
  • the amount of alkaline salt in the food raw material to which the enzyme is added is, for example, 0.0000000001 to 1.0% by weight, preferably 0.000000001 to 0.1% by weight, more preferably 0.00000001 to 0.06% by weight, and even more preferably 0.0000001 to 0.01% by weight per 1 g of protein.
  • the amount of calcium salt or calcium oxide in the food ingredient to which the enzyme is added is, for example, 0.0000000001 to 1.0% by weight, preferably 0.000000001 to 0.1% by weight, more preferably 0.00000001 to 0.06% by weight, and even more preferably 0.0000001 to 0.01% by weight per 1 g of protein.
  • the amount of magnesium salt or magnesium oxide in the food raw material to which the enzyme is added is, for example, 0.0000000001 to 0.1% by weight, preferably 0.000000001 to 0.05% by weight, more preferably 0.00000001 to 0.01% by weight, and even more preferably 0.0000001 to 0.001% by weight, per 1 g of protein.
  • the amount of reducing agent in the food raw material to which the enzyme is added is, for example, 0.000000000001 to 1.0% by weight, preferably 0.00000000001 to 0.5% by weight, more preferably 0.0000000001 to 0.1% by weight, and even more preferably 0.000000001 to 0.06% by weight, per 1 g of protein.
  • the amount of metal ions in the food raw material to which the enzyme is added is, for example, 0.0000000001 to 1.0% by weight, preferably 0.000000001 to 0.5% by weight, more preferably 0.00000001 to 0.1% by weight, and even more preferably 0.0000001 to 0.06% by weight per 1 g of protein.
  • the amount of the nonpolar amino acid or nonpolar amino acid salt in the food raw material to which the enzyme is added is, for example, 0.000000000001 to 1.0% by weight, preferably 0.00000000001 to 0.5% by weight, more preferably 0.0000000001 to 0.1% by weight, and even more preferably 0.000000001 to 0.06% by weight per 1 g of protein.
  • the amount of uncharged amino acid or uncharged amino acid salt in the food raw material to which the enzyme is added, and the amount of uncharged amino acid salt, per 1 g of protein is, for example, 0.00000000000001 to 1.0% by weight, preferably 0.000000000001 to 0.1% by weight, more preferably 0.000000000001 to 0.06% by weight, and even more preferably 0.00000000001 to 0.01% by weight.
  • the amount of basic amino acid or basic amino acid salt in the food raw material to which the enzyme is added is, for example, 0.0000000001 to 0.1% by weight, preferably 0.000000001 to 0.05% by weight, more preferably 0.00000001 to 0.01% by weight, and even more preferably 0.0000001 to 0.001% by weight, per 1 g of protein.
  • the amount of the acidic amino acid or acidic amino acid salt in the food raw material to which the enzyme is added is, for example, 0.0000000001 to 0.1% by weight, preferably 0.000000001 to 0.05% by weight, more preferably 0.00000001 to 0.01% by weight, and even more preferably 0.0000001 to 0.001% by weight, per 1 g of protein.
  • the manufacturing method of the present invention can be manufactured by the same method using the same raw materials as ordinary protein-containing foods, except that the raw materials are treated with the enzyme of the present invention (when ascorbic acid oxidase or glucose oxidase is used, ascorbic acids or glucose as a substrate are included in the raw materials) and/or, preferably, the auxiliary materials described above are used.
  • the enzyme of the present invention may be allowed to act on the food raw materials at any stage of the manufacturing process of the protein-containing food. It may also be added and allowed to act in the process of manufacturing the protein raw materials.
  • the enzyme of the present invention can be allowed to act on the food raw materials by coexisting with the food raw materials as it is, or by preparing an appropriate solution, etc.
  • the enzyme of the present invention may be added to the food raw materials, or the food raw materials may be immersed in a treatment solution containing the enzyme of the present invention.
  • additional such an operation of coexisting the enzyme of the present invention with the food raw materials is collectively referred to as "addition" of the enzyme of the present invention.
  • the enzymes in the present invention may be added to the food raw material all at the same time and allowed to act, or may be added to the food raw material separately, or in any combination, and allowed to act. Treatment with the enzyme preparation of the present invention described below can also be carried out in the same manner.
  • modified protein-containing foods refers to imparting or enhancing a favorable texture (smoothness, hardness, elasticity).
  • modification also includes suppression of an unusual taste or flavor or suppression of an unpleasant taste through modification. The presence or absence of modification can be evaluated according to the sensory evaluation in the test examples described below.
  • the present invention also relates to an enzyme preparation for modifying protein-containing foods, which contains phospholipase D (hereinafter, also simply referred to as the enzyme preparation of the present invention).
  • the definition and examples of protein-containing foods, examples of protein-containing food raw materials, examples of auxiliary materials, the amount of auxiliary materials in the food raw materials, and the definition, amount to be added, and method of addition (action time, action temperature, method of terminating the enzyme reaction) of phospholipase D are the same as the definition and examples of protein-containing foods, examples of protein-containing food raw materials, examples of auxiliary materials, the amount of auxiliary materials in the food raw materials, and the definition, amount to be added, and method of addition (action time, action temperature, method of terminating the enzyme reaction) of phospholipase D in the production method of the present invention.
  • the enzyme preparation of the present invention preferably further contains an enzyme that contributes to the formation of a crosslinked structure in addition to the above-mentioned phospholipase D.
  • the definition, examples, amount to be added, and method of addition of the enzyme that contributes to the formation of a crosslinked structure are the same as the definition, examples, amount to be added, and method of addition of the enzyme that contributes to the formation of a crosslinked structure in the production method of the present invention.
  • the enzyme preparation of the present invention can be added to a protein-containing food raw material (preferably a food raw material further containing the above-mentioned auxiliary materials) in accordance with the method and amount of addition of phospholipase D (or phospholipase D and an enzyme that contributes to the formation of a cross-linked structure) described in the production method of the present invention above, and allowed to react to produce a modified protein-containing food.
  • the enzyme preparation of the present invention can also be used as a pickling solution for meat processing, for example, for modifying proteins in processed meat foods as described below.
  • the present invention also relates to a pickling solution for meat processing (hereinafter simply referred to as the pickling solution of the present invention) containing phospholipase D for modifying proteins in processed meat foods.
  • processed meat products include ham, sausage, hamburger steak, fried chicken, etc.
  • the definition, amount to be added, and method of addition (action time, action temperature, and method of terminating the enzyme reaction) of phospholipase D are the same as those of phospholipase D in the production method of the present invention.
  • the pickling liquor of the present invention preferably further contains an enzyme contributing to the formation of a crosslinked structure in addition to the above-mentioned phospholipase D.
  • the definition, examples, amount to be added, and method of addition of the enzyme contributing to the formation of a crosslinked structure in the pickling liquor of the present invention are the same as the definition, examples, amount to be added, and method of addition of the enzyme contributing to the formation of a crosslinked structure in the production method of the present invention.
  • the pickling liquor of the present invention may contain additives commonly used in pickling liquors (e.g., salt, sugars (reduced starch syrup), polymerized phosphates, nitrites, sodium ascorbate, gelling agents (e.g., carrageenan), heterogeneous proteins (e.g., egg white, soy protein, milk protein, sodium caseinate), seasonings (e.g., AJINOMOTO (trade name)), and coloring agents).
  • the amounts of the additives can be appropriately selected from the known amounts used in pickling liquors.
  • the amount of the pickling liquid of the present invention to be used may be appropriately selected so that the enzyme of the present invention is present in the above-mentioned preferred amount relative to the food material of the processed meat food to be treated.
  • the pickling solution of the present invention or the food raw material of the processed meat food to be treated preferably contains an auxiliary material selected from the above-mentioned (A) to (I). These auxiliary materials may be contained alone or in combination of two or more.
  • the examples of auxiliary materials and the amounts of auxiliary materials blended in the food raw material are the same as the examples of auxiliary materials and the amounts of auxiliary materials blended in the food raw material in the production method of the present invention.
  • the present invention also relates to a method for modifying protein-containing foods (hereinafter also simply referred to as the modification method of the present invention), which comprises treating a protein-containing food raw material with phospholipase D.
  • the definition and examples of protein-containing foods, examples of protein-containing food raw materials, examples of auxiliary materials, the amount of auxiliary materials added in the food raw materials, and the definition, amount added, and method of addition (action time, action temperature, method of terminating the enzyme reaction) of phospholipase D are the same as the definition and examples of protein-containing foods, examples of protein-containing food raw materials, examples of auxiliary materials, the amount of auxiliary materials added in the food raw materials, and the definition, amount added, and method of addition (action time, action temperature, method of terminating the enzyme reaction) of phospholipase D in the production method of the present invention.
  • the modification method of the present invention it is preferable to further add an enzyme that contributes to the formation of a crosslinked structure to the food raw material and allow it to act in addition to the above-mentioned phospholipase D.
  • the definition, examples, amount added, and method of addition of the enzyme that contributes to the formation of a crosslinked structure are the same as the definition, examples, amount added, and method of addition of the enzyme that contributes to the formation of a crosslinked structure in the production method of the present invention.
  • Hardness compared to the control, 5 points: very hard texture. 4 points: hard texture. 3 points: The texture is a little hard. 2 points: equal. 1 point: Soft texture.
  • Unusual taste/flavor Compared to the control, ⁇ : No unusual taste/flavor was detected. ⁇ : There is a slight strange taste or flavor. ⁇ : An unusual taste or flavor is felt.
  • Hardness As ham, 5 points: The texture is very hard and pleasant. 4 points: The texture is firm and pleasant. 3 points: The texture is slightly hard and preferable. 2 points: Normal texture. 1 point: The texture is soft and undesirable.
  • Off-flavor/flavor As ham, ⁇ : No strange taste or flavor is detected. ⁇ : There is a slight strange taste or flavor. ⁇ : An unusual taste or flavor is felt.
  • sample 3-4 which is a mixture of egg white, soy protein, milk protein, and sodium caseinate to which a PLD preparation and a TG preparation have been added, has improved smoothness, hardness, and elasticity compared to sample 3-2 (control).
  • Hardness As a chikuwa 5 points: The texture is very hard and pleasant. 4 points: The texture is firm and pleasant. 3 points: The texture is slightly hard and preferable. 2 points: Normal texture. 1 point: The texture is soft and undesirable.
  • Hardness As a chikuwa 5 points: The texture is very hard and pleasant. 4 points: The texture is firm and pleasant. 3 points: The texture is slightly hard and preferable. 2 points: Normal texture. 1 point: The texture is soft and undesirable.
  • Hardness As kamaboko, 5 points: The texture is very hard and pleasant. 4 points: The texture is firm and pleasant. 3 points: The texture is slightly hard and preferable. 2 points: Normal texture. 1 point: The texture is soft and undesirable.
  • Test Example 7 Confirmation of the Effect of Adding Phospholipase D to a Soy Gel System Soy gels, Samples 7-1 to 7-10, were prepared according to the sample preparation flow shown in Figure 7 using the blending recipes shown in Table 15. The prepared samples exhibited the properties of either a suspension, a sol, or a gel. For the obtained samples 7-1 to 7-10, four expert panelists performed a sensory evaluation of smoothness according to the following evaluation criteria. The results are shown in Table 16.
  • Hardness As a chikuwa 5 points: The texture is very hard and pleasant. 4 points: The texture is firm and pleasant. 3 points: The texture is slightly hard and preferable. 2 points: Normal texture. 1 point: The texture is soft and undesirable.
  • Sample 8-2 in which a part of the raw material frozen surimi (trade name: Alaska pollock land grade 2) of Sample 8-1 was replaced with a low-grade frozen surimi (trade name: hairtail), was used.
  • Sample 8-5 in which the entire amount of the frozen surimi (product name: Alaska pollock land grade 2) used as the raw material in Sample 8-1 was replaced with a low-grade frozen surimi (product name: hairtail), the smoothness, hardness, and elasticity were further deteriorated.
  • the chikuwa of sample 8-3 which was produced by adding a PLD preparation to a chikuwa material containing soy protein, had improved smoothness compared to sample 8-2 (control).
  • the chikuwa of sample 8-4 which was produced by adding a PLD preparation and a TG preparation to a chikuwa material containing soy protein, had improved smoothness, hardness, and elasticity compared to sample 8-2 (control).
  • the chikuwa of sample 8-6 which was produced by adding a PLD preparation to a chikuwa material containing soy protein, had improved smoothness and elasticity compared to sample 8-5 (control).
  • the chikuwa of sample 8-7 which was produced by adding a PLD preparation and a TG preparation to a chikuwa material containing soy protein, had improved smoothness, hardness, and elasticity compared to sample 8-5 (control).
  • Hardness As a chikuwa 5 points: The texture is very hard and pleasant. 4 points: The texture is firm and pleasant. 3 points: The texture is slightly hard and preferable. 2 points: Normal texture. 1 point: The texture is soft and undesirable.
  • sample 9-2 in which part of the frozen minced fish (product name: Alaska pollock land grade 2) used as the raw material in sample 9-1 was replaced with soy protein, had a worsening of smoothness.
  • the chikuwa of sample 9-3 which was produced by adding a PLD preparation to a chikuwa material containing soy protein, had improved smoothness compared to sample 9-2 (control).
  • the chikuwa of sample 9-4 which was produced by adding a PLD preparation and a TG preparation to a chikuwa material containing soy protein, had improved smoothness, hardness, and elasticity compared to sample 9-2 (control).
  • Test Example 10 Confirmation of the effect of adding phospholipase D to cheese analogues Using the recipe shown in Table 21, the raw materials were emulsified by heating with stirring at 70°C for 5 minutes (enzyme reaction step) using a heating stirrer (Thermomix (trade name), manufactured by Vorwek). Then, the raw materials were heated with stirring at 90°C for 8 minutes (enzyme inactivation step). The resulting mixture was filled into a mold and cooled in a refrigerator (5°C) for 48 hours to prepare cheese analogues of Samples 10-1 to 10-6. For the obtained Samples 10-1 to 10-6, a sensory evaluation of smoothness was carried out by three expert panelists according to the following evaluation criteria. The results are shown in Table 22.
  • the mixture was spread, combined, and rolled in a noodle machine (small continuous rolling noodle machine, manufactured by Sodick Co., Ltd.) to obtain buckwheat dough.
  • the obtained buckwheat dough was cut out using a cutting blade of #20, and 70 g of the cut noodles were wrapped in packaging vinyl and frozen at -25 ° C.
  • the frozen noodles were stored at -18 ° C.
  • the frozen noodles were boiled in hot water for 2 minutes, then drained, cooled, and drained to prepare Chinese noodles samples 11-1 to 11-5.
  • the obtained samples 11-1 to 11-5 were divided into containers and a loosening agent "SOYAUP M3000" (Fuji Oil Co., Ltd.) was added in an amount of 3% by weight of the noodles. After storing in a refrigerator at 10° C. or below for 2 days, the noodles were loosened in cold noodle soup in an amount of 33% by weight of the noodles, and a sensory evaluation was carried out. The sensory evaluation was carried out by five expert panelists in accordance with the following criteria for smoothness, hardness, elasticity, and off-flavors. The results are shown in Table 24.
  • Hardness As Chinese noodles, 5 points: The texture is very hard and pleasant. 4 points: The texture is firm and pleasant. 3 points: The texture is slightly hard and preferable. 2 points: Normal texture. 1 point: The texture is soft and undesirable.
  • Tables 28-1 and 28-2 show that samples 12-3 to 12-15, in which the PLD preparation was added so that the enzyme activity per gram of protein in the sample was in the range of 0.00000065 to 6494.3 U, showed improved smoothness compared to sample 12-2 (control).
  • Samples 13-A1-2 to 13-A1-7 which contained PLD and sodium carbonate, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-A1-2 to 13-A1-7 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no sodium carbonate. From the results in Table 30-3, Samples 13-A2-2 to 13-A2-9, which contained PLD and trisodium phosphate, showed improved smoothness compared to Sample 13-2 (control).Also, Samples 13-A2-2 to 13-A2-9 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no trisodium phosphate.
  • Samples 13-A3-2 and 13-A3-3 which contained PLD and tripotassium phosphate, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-A3-2 and 13-A3-3 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no tripotassium phosphate. From the results in Table 30-5, Sample 13-A4-2, to which PLD and trisodium citrate were added, had improved smoothness compared to Sample 13-2 (control). Sample 13-A4-2 also had improved smoothness compared to Sample 13-3 (see Table 30-1), to which PLD was added but trisodium citrate was not added.
  • Samples 13-B1-2 to 13-B1-9 which contained PLD and calcium chloride, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-B1-2 to 13-B1-9 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but not calcium chloride. From the results of Table 30-7, Samples 13-B2-2 to 13-B2-7, which contained PLD and calcined shell calcium, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-B2-2 to 13-B2-7 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no calcined shell calcium.
  • Samples 13-B3-3 and 13-B3-4 which contained PLD and calcium lactate, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-B3-3 and 13-B3-4 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but not calcium lactate. From the results of Table 30-9, Samples 13-B4-2 and 13-B4-3, which contained PLD and calcium carbonate, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-B4-2 and 13-B4-3 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no calcium carbonate.
  • Samples 13-C1-2 to 13-C1-8 which contained PLD and magnesium chloride, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-C1-2 to 13-C1-8 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no magnesium chloride. From the results in Table 30-11, Samples 13-C2-2 and 13-C2-3, which contained PLD and magnesium glutamate, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-C2-2 and 13-C2-3 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no magnesium glutamate.
  • Samples 13-D1-2 to 13-D1-9 which contained PLD and glutathione-containing yeast extract, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-D1-2 to 13-D1-9 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no glutathione-containing yeast extract.
  • Samples 13-D2-2 to 13-D2-10 which contained PLD and cysteine-containing yeast extract, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-D2-2 to 13-D2-10 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no cysteine-containing yeast extract.
  • Samples 13-E1-2 to 13-E1-9 which contained PLD and iron-containing yeast, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-E1-2 to 13-E1-9 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no iron-containing yeast. From the results of Table 30-15, samples 13-E2-3 to 13-E2-6, which contained PLD and copper-containing yeast, showed improved smoothness compared to sample 13-2 (control). Also, samples 13-E2-3 to 13-E2-6 showed improved smoothness compared to sample 13-3 (see Table 30-1), which contained PLD but no copper-containing yeast.
  • samples 13-E3-2 to 13-E3-7 which contained PLD and manganese-containing yeast, showed improved smoothness compared to sample 13-2 (control). Also, samples 13-E3-2 to 13-E3-7 showed improved smoothness compared to sample 13-3 (see Table 30-1), which contained PLD but no manganese-containing yeast. From the results of Table 30-17, Samples 13-F1-2 to 13-F1-7, which contained PLD and glycine, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-F1-2 to 13-F1-7 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but not glycine.
  • Samples 13-F2-2 to 13-F2-9 which contained PLD and cystine, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-F2-2 to 13-F2-9 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no cystine. From the results in Table 30-19, samples 13-F3-2 and 13-F3-3 to which PLD and alanine were added showed improved smoothness compared to sample 13-2 (control). Also, samples 13-F3-2 and 13-F3-3 showed improved smoothness compared to sample 13-3 to which PLD was added but no alanine was added (see Table 30-1).
  • Samples 13-F4-2 to 13-F4-3 to which PLD and valine were added had improved smoothness compared to Sample 13-2 (control). Also, Samples 13-F4-2 to 13-F4-3 had improved smoothness compared to Sample 13-3 to which PLD was added but no valine was added (see Table 30-1). From the results of Table 30-21, Samples 13-F5-2 and 13-F5-3, which contained PLD and leucine, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-F5-2 and 13-F5-3 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no leucine.
  • Samples 13-F6-2 and 13-F6-3 which contained PLD and isoleucine, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-F6-2 and 13-F6-3 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but not isoleucine. From the results in Table 30-23, Samples 13-F7-3 and 13-F7-4, which contained PLD and phenylalanine, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-F7-3 and 13-F7-4 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no phenylalanine.
  • samples 13-F8-3 and 13-F8-4 to which PLD and proline were added had improved smoothness compared to sample 13-2 (control). Also, samples 13-F8-3 and 13-F8-4 had improved smoothness compared to sample 13-3 to which PLD was added but not proline (see Table 30-1). From the results of Table 30-25, Samples 13-F9-2 and 13-F9-3, which contained PLD and methionine, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-F9-2 and 13-F9-3 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no methionine.
  • samples 13-G5-3 to 13-G5-5 to which PLD and cysteine were added had improved smoothness compared to sample 13-2 (control). Also, samples 13-G5-3 to 13-G5-5 had improved smoothness compared to sample 13-3 to which PLD was added but no cysteine was added (see Table 30-1). From the results in Table 30-31, Samples 13-G6-3 to 13-G6-7, which contained PLD and cysteine hydrochloride, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-G6-3 to 13-G6-7 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no cysteine hydrochloride.
  • Samples 13-I2-3 to 13-I2-4 which contained PLD and sodium glutamate, showed improved smoothness compared to Sample 13-2 (control). Also, Samples 13-I2-3 to 13-I2-4 showed improved smoothness compared to Sample 13-3 (see Table 30-1), which contained PLD but no sodium glutamate.
  • Samples 14A-6 to 14A-14 and Samples 14B-6 to 14B-14 which contained PLD and ASO, showed improved smoothness compared to Sample 14-2 (control). Also, Samples 14A-6 to 14A-14 and Samples 14B-6 to 14B-14 showed improved smoothness compared to Sample 14-3 (see Table 32-1), which contained PLD but no ASO. From the results of Tables 32-4 and 32-5, Samples 14C-6 to 14C-11 and Samples 14D-6 to 14D-11, which contained PLD and GO, showed improved smoothness compared to Sample 14-2 (control). Also, Samples 14C-6 to 14C-11 and Samples 14D-6 to 14D-11 showed improved smoothness compared to Sample 14-3 (see Table 32-1), which contained added PLD and no added GO.
  • Sample 15A-2 in which PLD was added to oat protein (PLD activity value: 297.4 U/1 g of protein), showed improved smoothness compared to sample 15A-1 (control).
  • Sample 15A-4 in which PLD was added to oat protein (PLD activity value: 29.7 U/1 g of protein), showed improved smoothness compared to sample 15A-3 (control).
  • Sample 15A-12 in which PLD was added to oat protein (PLD activity: 14.9 U/g protein), had improved smoothness compared to sample 15A-11 (control).
  • Sample 15B-2 in which PLD was added to pea protein (PLD activity value: 215.4 U/g of protein), showed improved smoothness compared to sample 15B-1 (control).
  • Sample 15B-4 in which PLD was added to pea protein (PLD activity value: 21.5 U/g of protein), showed improved smoothness compared to sample 15B-3 (control).
  • Sample 15B-12 in which PLD was added to pea protein (PLD activity value: 10.8 U/g of protein), showed improved smoothness compared to sample 15B-11 (control).
  • Sample 15C-2 in which PLD was added to broad bean protein (PLD activity value: 201.8 U/g protein), showed improved smoothness compared to sample 15C-1 (control).
  • Sample 15C-4 in which PLD was added to broad bean protein (PLD activity value: 20.2 U/1 g of protein), showed improved smoothness compared to sample 15C-3 (control).
  • Sample 15C-12 in which PLD was added to broad bean protein (PLD activity value: 10.1 U/g of protein), showed improved smoothness compared to sample 15C-11 (control).
  • Sample 15D-2 in which PLD was added to mung bean protein (PLD activity value: 226.0 U/1 g of protein), showed improved smoothness compared to sample 15D-1 (control).
  • Sample 15D-4 (PLD activity 22.6 U/1 g protein), in which PLD was added to mung bean protein, showed improved smoothness compared to sample 15D-3 (control).
  • Sample 15D-12 in which PLD was added to mung bean protein (PLD activity value: 11.3 U/g of protein), showed improved smoothness compared to sample 15D-11 (control).
  • Sample 15E-2 in which PLD was added to rice protein (PLD activity value: 226.0 U/g of protein), had improved smoothness compared to sample 15E-1 (control).
  • Sample 15E-4 in which PLD was added to rice protein (PLD activity value: 22.6 U/g of protein), showed improved smoothness compared to sample 15E-3 (control).
  • Sample 15E-12 in which PLD was added to rice protein (PLD activity value: 11.3 U/g of protein), showed improved smoothness compared to sample 15E-11 (control).
  • Sample 15F-2 in which PLD was added to chickpea protein (PLD activity value: 269.0 U/1 g of protein), showed improved smoothness compared to sample 15F-1 (control).
  • Sample 15F-4 in which PLD was added to chickpea protein (PLD activity value: 26.9 U/1 g of protein), showed improved smoothness compared to sample 15F-3 (control).
  • Sample 15F-12 in which PLD was added to chickpea protein (PLD activity: 13.5 U/1 g of protein), showed improved smoothness compared to sample 15F-11 (control).
  • Sample 15G-4 PLD activity 18.8 U/g protein), in which PLD was added to rapeseed protein, showed improved smoothness compared to sample 15G-3 (control).
  • Sample 15G-12 (PLD activity 9.4 U/g protein), in which PLD was added to rapeseed protein, showed improved smoothness compared to sample 15G-11 (control).
  • Sample 15H-2 in which PLD was added to egg white (PLD activity value: 204.2 U/g of protein), showed improved smoothness compared to sample 15H-1 (control).
  • Sample 15H-4 in which PLD was added to egg white (PLD activity value: 20.4 U/g of protein), showed improved smoothness compared to sample 15H-3 (control).
  • Sample 15H-12 in which PLD was added to egg white (PLD activity value: 10.2 U/g of protein), showed improved smoothness compared to sample 15H-11 (control).
  • Sample 15I-2 in which PLD was added to corn protein (PLD activity value: 1461.2 U/g of protein), showed improved smoothness compared to sample 15I-1 (control).
  • Sample 15I-4 in which PLD was added to corn protein (PLD activity value: 146.1 U/1 g of protein), showed improved smoothness compared to sample 15I-3 (control).
  • Sample 15I-12 in which PLD was added to corn protein (PLD activity value: 73.1 U/1 g of protein), showed improved smoothness compared to sample 15I-11 (control).
  • Sample 15J-2 in which PLD was added to whey protein (PLD activity value: 1,356.0 U/g of protein), showed improved smoothness compared to sample 15J-1 (control).
  • Sample 15J-4 in which PLD was added to whey protein (PLD activity value: 135.6 U/1 g of protein), showed improved smoothness compared to sample 15J-3 (control).
  • Sample 15J-12 (PLD activity 67.8 U/g protein), in which PLD was added to whey protein, showed improved smoothness compared to sample 15J-11 (control).
  • Sample 15K-2 (PLD activity 625.5 U/g protein), in which PLD was added to whole milk powder protein, showed improved smoothness compared to sample 15K-1 (control).
  • Sample 15K-4 (PLD activity 62.5 U/g protein), in which PLD was added to whole milk powder protein, showed improved smoothness compared to sample 15K-3 (control).
  • Sample 15K-12 (PLD activity 31.3 U/g protein), in which PLD was added to whole milk powder protein, showed improved smoothness compared to sample 15K-11 (control).
  • Sample 15L-2 in which PLD was added to skim milk powder protein (PLD activity value: 476.1 U/1 g of protein), had improved smoothness compared to sample 15L-1 (control).
  • Sample 15L-4 (PLD activity 47.6 U/1 g protein), in which PLD was added to skim milk powder protein, had improved smoothness compared to sample 15L-3 (control).
  • Sample 15L-12 (PLD activity 23.8 U/1 g protein), in which PLD was added to skim milk powder protein, showed improved smoothness compared to sample 15L-11 (control).
  • Sample 15M-2 in which PLD was added to large-scale dehydrated protein (PLD activity value 767.0 U/1 g of protein), showed improved smoothness compared to sample 15M-1 (control).
  • Sample 15M-4 PLD activity 76.7 U/1 g protein
  • Sample 15M-12 in which PLD was added to large-scale dehydrated protein (PLD activity value: 38.3 U/1 g of protein), showed improved smoothness compared to sample 15M-11 (control).
  • Sample 15N-2 in which PLD was added to almond protein (PLD activity: 385.2 U/g of protein), showed improved smoothness compared to sample 15N-1 (control).
  • Sample 15N-4 in which PLD was added to almond protein (PLD activity value: 38.5 U/g of protein), showed improved smoothness compared to sample 15N-3 (control).
  • Sample 15N-12 in which PLD was added to almond protein (PLD activity value: 19.3 U/g of protein), showed improved smoothness compared to sample 15N-11 (control).
  • Sample 15O-2 in which PLD was added to peanut protein (PLD activity: 368.5 U/g of protein), showed improved smoothness compared to sample 15O-1 (control).
  • Sample 15O-4 in which PLD was added to peanut protein (PLD activity: 36.8 U/1 g of protein), showed improved smoothness compared to sample 15O-3 (control).
  • Sample 15O-12 in which PLD was added to peanut protein (PLD activity value: 18.4 U/1 g of protein), showed improved smoothness compared to sample 15O-11 (control).
  • Sample 15P-2 in which PLD was added to Cricket protein (PLD activity: 327.9 U/1 g of protein), showed improved smoothness compared to sample 15P-1 (control).
  • Sample 15P-4 in which PLD was added to Cricket protein (PLD activity value: 32.8 U/1 g of protein), showed improved smoothness compared to sample 15P-3 (control).
  • Sample 15P-12 in which PLD was added to Cricket protein (PLD activity value: 16.4 U/1 g of protein), showed improved smoothness compared to sample 15P-11 (control).
  • Sample 15Q-2 in which PLD was added to Big Cricket protein (PLD activity value: 306.5 U/1 g of protein), showed improved smoothness compared to sample 15Q-1 (control).
  • Sample 15Q-4 in which PLD was added to Big Cricket protein (PLD activity value: 30.7 U/1 g of protein), showed improved smoothness compared to sample 15Q-3 (control).
  • Sample 15Q-12 in which PLD was added to Big Cricket protein (PLD activity value: 15.3 U/1 g of protein), showed improved smoothness compared to sample 15Q-11 (control).
  • Sample 15R-2 in which PLD was added to silkworm protein (PLD activity: 309.9 U/g of protein), showed improved smoothness compared to sample 15R-1 (control).
  • Sample 15R-4 in which PLD was added to silkworm protein (PLD activity value: 31.0 U/1 g of protein), showed improved smoothness compared to sample 15R-3 (control).
  • Sample 15R-12 in which PLD was added to silkworm protein (PLD activity value: 15.5 U/1 g of protein), showed improved smoothness compared to sample 15R-11 (control).
  • Sample 15S-2 in which PLD was added to spirulina protein (PLD activity value: 274.3 U/g of protein), showed improved smoothness compared to sample 15S-1 (control).
  • Sample 15S-4 in which PLD was added to spirulina protein (PLD activity value: 27.4 U/g of protein), showed improved smoothness compared to sample 15S-3 (control).
  • Sample 15S-12 in which PLD was added to spirulina protein (PLD activity value: 13.7 U/g of protein), showed improved smoothness compared to sample 15S-11 (control).
  • samples 15L-5 to 15L-10 in which PLD and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, alanine, cysteine hydrochloride, or cysteine) were added to skim milk powder protein, had improved smoothness compared to sample 15L-4, in which PLD was added but no auxiliary materials were added.
  • Samples 16A-2 to 16A-8 in which PLD was added to soy milk, showed improved smoothness compared to Sample 16A-1 (control). Also, Samples 16A-3 to 16A-8, in which PLD and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, alanine, cysteine hydrochloride, or cysteine) were added to soy milk, showed improved smoothness compared to Sample 16A-2, in which PLD was added but no auxiliary materials were added. From the results in Table 36-2, samples 16B-2 to 16B-8, in which PLD was added to oat milk, showed improved smoothness compared to sample 16B-1 (control).
  • samples 16B-3 to 16B-8 in which PLD and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, alanine, cysteine hydrochloride, or cysteine) were added to oat milk, showed improved smoothness compared to sample 16B-2, in which PLD was added but no auxiliary materials were added. From the results of Table 36-3, samples 16C-2 to 16C-8, in which PLD was added to coconut milk, had improved smoothness compared to sample 16C-1 (control).
  • samples 16C-3 to 16C-8 in which PLD and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, alanine, cysteine hydrochloride, or cysteine) were added to coconut milk, had improved smoothness compared to sample 16C-2, in which PLD was added but no auxiliary materials were added.
  • samples 17A-2 to 17A-8 which were prepared by adding PLD to beef belly meat (lean meat only), showed improved smoothness compared to sample 17A-1 (control). Also, samples 17A-3 to 17A-8, which were prepared by adding PLD and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, alanine, cysteine hydrochloride, or cysteine) to beef belly meat (lean meat only), showed improved smoothness compared to sample 17A-2, which was prepared by adding PLD but not adding the auxiliary materials.
  • samples 17B-2 to 17B-8 in which PLD was added to pork shoulder meat (lean meat only), showed improved smoothness compared to sample 17B-1 (control). Also, samples 17B-3 to 17B-8, in which PLD and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, alanine, cysteine hydrochloride, or cysteine) were added to pork shoulder meat (lean meat only), showed improved smoothness compared to sample 17B-2, in which PLD was added but no auxiliary materials were added. From the results of Table 38-3, samples 17C-2 to 17C-8, in which PLD was added to chicken breast meat, showed improved smoothness compared to sample 17C-1 (control).
  • samples 17C-3 to 17C-8 in which PLD and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, alanine, cysteine hydrochloride, or cysteine) were added to chicken breast meat, showed improved smoothness compared to sample 17C-2, in which PLD was added but no auxiliary materials were added.
  • Protein gels of Samples 18A-1 to 18A-6 were prepared according to the blending recipe shown in Table 39-1 and the sample preparation flow shown in Figure 12 (without the sitting process (generally a process in which meat paste is left at a low temperature of approximately 10 to 40°C for a certain period of time)). The prepared samples exhibited the properties of either a suspension, a sol, or a gel.
  • protein gels of Samples 18B-1 to 18B-6 were prepared using the formulation recipe shown in Table 39-2 and in accordance with the sample preparation flow (including a sitting step) shown in FIG. For each of the obtained samples, a sensory evaluation of smoothness was carried out by three expert panelists according to the following evaluation criteria. The results are shown in Tables 40-1 and 40-2.
  • samples 18A-2 to 18A-6 which were obtained by adding PLD to hairtail C, showed improved smoothness compared to sample 18A-1 (control).
  • samples 18A-3 to 18A-6 which were obtained by adding PLD and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, or cysteine hydrochloride) to hairtail C, showed improved smoothness compared to sample 18A-2, which was obtained by adding PLD and not adding the auxiliary materials.
  • samples 18B-2 to 17B-6 which were obtained by adding PLD to hairtail C, showed improved smoothness compared to sample 18B-1 (control).
  • samples 18B-3 to 18B-6 which were obtained by adding PLD and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, or cysteine hydrochloride) to hairtail C, showed improved smoothness compared to sample 18B-2, which was obtained by adding PLD and not adding the auxiliary materials.
  • Unusual taste/flavor Compared to the control, ⁇ : No unusual taste/flavor was detected. ⁇ : An unusual taste or flavor is felt.
  • Tables 42-1 and 42-2 show that samples 19-12 to 19-14, in which PLD was added to soy gel, had improved smoothness compared to sample 19-1 (control).
  • samples that used high amounts of lecithin, PLA1, or PLA2 had an unpleasant taste or flavor
  • samples 19-12 to 19-14, in which PLD was added were superior in that they had high scores for smoothness and did not have an unpleasant taste or flavor.
  • samples 21-2 to 21-9 in which PLD was added to the hamburger steak, had improved smoothness compared to sample 21-1 (control). Also, samples 21-3 to 21-9, in which PLD and auxiliary ingredients (threonine, manganese-containing yeast, glutathione-containing yeast extract, glycine, alanine, cysteine hydrochloride, or cysteine) were added to the hamburger steak, had improved smoothness compared to sample 21-2, in which PLD was added but no auxiliary ingredients were added.
  • PLD and auxiliary ingredients threonine, manganese-containing yeast, glutathione-containing yeast extract, glycine, alanine, cysteine hydrochloride, or cysteine
  • samples 22-2 through 22-9 in which PLD was added to the hamburger steak, had improved smoothness compared to sample 22-1 (control).
  • samples 22-3 through 22-9 in which PLD and auxiliary ingredients (threonine, manganese-containing yeast, glutathione-containing yeast extract, glycine, alanine, cysteine hydrochloride, or cysteine) were added to the hamburger steak, had improved smoothness compared to sample 22-2, in which PLD was added but no auxiliary ingredients were added.
  • Hardness As ham, 5 points: The texture is very hard and pleasant. 4 points: The texture is firm and pleasant. 3 points: The texture is slightly hard and preferable. 2 points: Normal texture. 1 point: The texture is soft and undesirable.
  • samples 23-4 to 23-11 which were made by adding PLD and TG preparations to a mixture of egg white, soy protein, milk protein, and sodium caseinate, showed improved smoothness, hardness, and elasticity compared to sample 23-2 (control). Furthermore, samples 23-5 to 23-11, which were further supplemented with auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, glycine, alanine, cysteine hydrochloride, or cysteine), showed improved smoothness compared to sample 23-4, which did not contain the above auxiliary materials.
  • auxiliary materials threonine, manganese-containing yeast, glutathione-containing yeast extract, glycine, alanine, cysteine hydrochloride, or cysteine
  • Test Example 24 Confirmation of Effect of Addition of Phospholipase D to Tofu Using the bittern liquid having the composition shown in Table 51 and the composition recipe shown in Table 52, tofu samples 24-1 to 24-8 were prepared according to the sample preparation flow shown in FIG. 16. For each of the obtained samples, a sensory evaluation of smoothness was performed by three expert panelists using Sample 24-1 as a control according to the same evaluation criteria as those in Test Example 12. The results are shown in Table 53.
  • Test Example 25 Confirmation of the effect of adding phospholipase D to plant-based (PB) cheese Samples 25-1 to 25-9 of PB cheese were prepared according to the blend recipe shown in Table 54 and the sample preparation flow shown in Figure 17. For each of the obtained samples, a sensory evaluation of smoothness was performed by three expert panelists, using sample 25-1 as a control, according to the same evaluation criteria as those in Test Example 12. The results are shown in Table 55.
  • samples 25-2 to 25-9 in which a PLD preparation was added to PB cheese, had improved smoothness compared to sample 25-1 (control).
  • samples 25-3 to 25-9 in which a PLD preparation and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, cysteine hydrochloride, glycine, alanine, or cysteine) were added to PB cheese, had improved smoothness compared to sample 25-2, in which a PLD preparation was added but no auxiliary materials were added.
  • Test Example 26 Confirmation of the effect of adding phospholipase D to PB yogurt Using the blending recipe shown in Table 56 and following the sample preparation flow shown in Figure 18, PB yogurt samples 26-1 to 26-9 were prepared. For each of the obtained samples, a sensory evaluation of smoothness was performed by three expert panelists, using Sample 26-1 as a control, according to the same evaluation criteria as those in Test Example 12. The results are shown in Table 57.
  • samples 26-2 to 26-9 in which a PLD preparation was added to PB yogurt, had improved smoothness compared to sample 26-1 (control). Also, samples 26-3 to 26-9, in which a PLD preparation and auxiliary ingredients (threonine, manganese-containing yeast, glutathione-containing yeast extract, cysteine hydrochloride, glycine, alanine, or cysteine) were added to PB yogurt, had improved smoothness compared to sample 26-2, in which a PLD preparation was added but no auxiliary ingredients were added.
  • samples 27-2 to 27-9 in which a PLD preparation was added to PB eggs, had improved smoothness compared to sample 27-1 (control).
  • samples 27-3 to 27-9 in which a PLD preparation and auxiliary materials (threonine, manganese-containing yeast, glutathione-containing yeast extract, cysteine hydrochloride, glycine, alanine, or cysteine) were added to PB eggs, had improved smoothness compared to sample 27-2, in which a PLD preparation was added but no auxiliary materials were added.
  • samples 28-2 to 28-9 in which a PLD preparation was added to the PB snack, had improved smoothness compared to sample 28-1 (control).
  • samples 28-3 to 28-9 in which a PLD preparation and auxiliary ingredients (threonine, manganese-containing yeast, glutathione-containing yeast extract, cysteine hydrochloride, glycine, alanine, or cysteine) were added to the PB snack, had improved smoothness compared to sample 28-2, in which a PLD preparation was added but no auxiliary ingredients were added.
  • samples 29-2 to 29-9 in which a PLD preparation was added to the PB snack, had improved smoothness compared to sample 29-1 (control).
  • samples 29-3 to 29-9 in which a PLD preparation and auxiliary ingredients (threonine, manganese-containing yeast, glutathione-containing yeast extract, cysteine hydrochloride, glycine, alanine, or cysteine) were added to the PB snack, had improved smoothness compared to sample 29-2, in which a PLD preparation was added but no auxiliary ingredients were added.
  • sample 31-4 which contains Chinese noodles with added PLD, has improved smoothness, hardness, and elasticity compared to sample 31-5 (control).
  • the present invention makes it possible to provide a protein-containing food product that improves the unpleasant texture that is derived from protein.

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Publication number Priority date Publication date Assignee Title
JPS6427471A (en) 1987-03-04 1989-01-30 Ajinomoto Kk Novel enzyme and production of protein gelatinized product using said enzyme
WO2010140708A1 (ja) * 2009-06-05 2010-12-09 味の素株式会社 畜肉加工製品改質用の酵素製剤及び畜肉加工製品の製造方法
WO2013172447A1 (ja) * 2012-05-17 2013-11-21 ナガセケムテックス株式会社 食品素材改質用酵素製剤
JP2016189708A (ja) * 2015-03-31 2016-11-10 興人ライフサイエンス株式会社 酵母由来呈味増強剤
WO2017154992A1 (ja) * 2016-03-10 2017-09-14 味の素株式会社 植物蛋白質含有食品の製造方法
WO2022231003A1 (ja) * 2021-04-30 2022-11-03 味の素株式会社 品質が向上した畜肉練り製品
JP2023022040A (ja) 2019-02-21 2023-02-14 デンカ株式会社 組成物

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* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS6427471A (en) 1987-03-04 1989-01-30 Ajinomoto Kk Novel enzyme and production of protein gelatinized product using said enzyme
WO2010140708A1 (ja) * 2009-06-05 2010-12-09 味の素株式会社 畜肉加工製品改質用の酵素製剤及び畜肉加工製品の製造方法
WO2013172447A1 (ja) * 2012-05-17 2013-11-21 ナガセケムテックス株式会社 食品素材改質用酵素製剤
JP2016189708A (ja) * 2015-03-31 2016-11-10 興人ライフサイエンス株式会社 酵母由来呈味増強剤
WO2017154992A1 (ja) * 2016-03-10 2017-09-14 味の素株式会社 植物蛋白質含有食品の製造方法
JP2023022040A (ja) 2019-02-21 2023-02-14 デンカ株式会社 組成物
WO2022231003A1 (ja) * 2021-04-30 2022-11-03 味の素株式会社 品質が向上した畜肉練り製品

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