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
  • A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
• • 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)
• • 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
  • 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
  • A23C11/106—Addition of, or treatment with, microorganisms
• • 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
  • A23J3/04—Animal proteins
• • 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
  • A23J3/04—Animal proteins
  • A23J3/08—Dairy proteins
• • 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
  • A23J3/04—Animal proteins
  • A23J3/08—Dairy proteins
  • A23J3/10—Casein
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
  • A23J3/00—Working-up of proteins for foodstuffs
  • A23J3/14—Vegetable proteins
  • A23J3/16—Vegetable proteins from soybean
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
  • A23J3/00—Working-up of proteins for foodstuffs
  • A23J3/14—Vegetable proteins
  • A23J3/18—Vegetable proteins from wheat
• • 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
  • 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
  • A23J3/343—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of dairy proteins
• • 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
  • A23J3/343—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of dairy proteins
  • A23J3/344—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of dairy proteins of casein
• • 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
  • A23L11/00—Pulses, i.e. fruits of leguminous plants, for production of food; Products from legumes; Preparation or treatment thereof
  • A23L11/50—Fermented pulses or legumes; Fermentation of pulses or legumes based on the addition of microorganisms
• • 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
  • A23L11/00—Pulses, i.e. fruits of leguminous plants, for production of food; Products from legumes; Preparation or treatment thereof
  • A23L11/60—Drinks from legumes, e.g. lupine drinks
• • 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
  • A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Preparation or treatment thereof
  • A23L2/52—Adding ingredients
  • A23L2/66—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
  • A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
  • A23L27/20—Synthetic spices, flavouring agents or condiments
  • A23L27/21—Synthetic spices, flavouring agents or condiments containing amino acids
• • 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
  • A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
  • A23L29/06—Enzymes
• • 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
  • C12Y101/00—Oxidoreductases acting on the CH-OH group of donors (1.1)
  • C12Y101/03—Oxidoreductases acting on the CH-OH group of donors (1.1) with a oxygen as acceptor (1.1.3)
  • C12Y101/0304—D-Mannitol oxidase (1.1.3.40)

Definitions

• the present invention relates to a method for producing a modified protein-containing liquid food, an enzyme preparation for modifying a protein-containing liquid food, and a method for modifying a protein-containing liquid food.
• Patent Document 1 discloses a soy milk-containing liquid food or drink, which is characterized in that 0.5 to 30 parts of coconut milk is mixed with 100 parts of soy milk and heat-treated at a temperature exceeding 100°C.
• Cited Document 2 discloses an oil-in-water emulsion for beverage additive, which contains (a) caseinate and (b) a milk raw material having a phospholipid content of 2% by mass or more in the milk-derived solid content, and in which (a)/(b) is 0.1 to 10 (wherein (a)/(b) is the mass ratio of the solid content). None of these documents describes the use of phospholipase D to improve the texture of protein-containing liquid foods.
• the object of the present invention is to provide a method for producing a protein-containing liquid food (particularly a food containing a relatively large amount of protein ingredients) with an improved unpleasant texture.
• the inventors conducted extensive research to solve the above problems and discovered that by adding a protein raw material and phospholipase D (sometimes referred to as "PLD” in this specification) during the manufacturing process of liquid foods such as beverages, a smooth texture can be imparted without imparting unpleasant textures such as “roughness” or “grittyness” that are derived from proteins. Based on this knowledge, the inventors conducted further research and completed the present invention.
• PLD protein raw material
• PLD phospholipase D
• the present invention is as follows.
• a method for producing a modified protein-containing liquid 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.
• [1-1] The method for producing the present invention according to any one of [1] to [11] above, further comprising treating the product with an enzyme that contributes to the formation of a crosslinked structure.
• a method for modifying a protein-containing liquid food comprising treating a protein-containing food raw material with phospholipase D.
• a protein-containing liquid food in which the unpleasant texture derived from protein is improved.
• a liquid food can be provided in which the unpleasant texture derived from protein 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 liquid foods, such as 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 the sample preparation flow in Test Examples 12, 13, 14, 15, 16, and 19.
• FIG. 8 shows a sample preparation flow in Test Example 17.
• FIG. 9 shows a sample preparation flow in Test Example 18.
• FIG. 10 shows a sample preparation flow in Test Example 20.
• the present invention relates to a method for producing a modified protein-containing liquid food.
• the method for producing an improved protein-containing liquid food of the present invention (hereinafter also referred to simply as the production method of the present invention) comprises treating a protein-containing food raw material with phospholipase D.
• protein-containing liquid foods include processed foods produced from protein-containing food ingredients (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 (for example, 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 whites, egg whites (powdered), milk protein, skimmed milk powder, whey powder, casein or a salt thereof (for example, sodium caseinate), cricket powder (Cricket, Big
• a "protein-containing liquid food” refers to a food that contains protein and is in a liquid state (in other words, in a fluid state).
• a "protein-containing liquid food” may be in a liquid state when consumed.
• foods that are sold in a powdered or solid state, etc., and that are dissolved or dispersed in water, hot water, etc. by the purchaser when consumed e.g., powdered drinks, solid drinks, powdered soups, solid soups
• protein-containing liquid foods examples include beverages (e.g., protein drinks, cafe au lait, plant-based milks (e.g., oat milk, almond milk, coconut milk, soy milk)), liquid seasonings (e.g., sauces, dressings), liquid processed foods (e.g., soups, liquid meals), and plant-based foods in which the animal protein in these liquid foods is replaced with plant protein (plant-based (PB) beverages).
• beverages e.g., protein drinks, cafe au lait, plant-based milks (e.g., oat milk, almond milk, coconut milk, soy milk)
• liquid seasonings e.g., sauces, dressings
• liquid processed foods e.g., soups, liquid meals
• plant-based (PB) beverages plant-based (PB) beverages).
• PB plant-based
• the form in which the protein-containing liquid food is provided is not particularly limited. That is, the protein-containing liquid food may be provided in any form, such as raw food, heated product, frozen product,
• a vegetable or animal-derived protein e.g., vegetable proteins such as soybean protein and wheat protein; animal proteins such as egg white, milk protein, casein or a salt thereof (e.g., sodium caseinate), cricket powder, etc.
• a product can be provided in which the unpleasant texture derived from protein is suppressed.
• 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 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% by weight, preferably 1 to 95% by weight, more preferably 5 to 90% by weight, and even more preferably 10 to 80% by weight, 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 (IV).
• (I) to (IV) are collectively referred to as "the enzymes in the present invention.
• (I) Phospholipase D Phospholipase D and ascorbate oxidase
• III Phospholipase D and glucose oxidase
• IV Phospholipase D, ascorbate oxidase, and glucose oxidase
• 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 liquid foods, except that the raw materials are treated with the enzyme of the present invention (when ascorbic acid oxidase or glucose oxidase is used, the raw materials contain ascorbic acids or glucose as substrates), and/or preferably the above-mentioned auxiliary materials 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 liquid 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 either as it is or by preparing an appropriate solution or the like and allowing it to coexist with the food raw materials.
• 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 operations of allowing the enzyme of the present invention to coexist with the food raw materials are collectively referred to as "addition" of the enzyme of the present invention.
• modified protein-containing liquid food refers to imparting or enhancing a favorable texture (smoothness).
• modification also includes suppressing an unusual taste or flavor or suppressing 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 liquid food, which contains phospholipase D (hereinafter, also simply referred to as the enzyme preparation of the present invention).
• the definition and examples of protein-containing liquid 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 liquid 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 liquid food.
• a protein-containing food raw material preferably a food raw material further containing the above-mentioned auxiliary materials
• the present invention also relates to a method for modifying a protein-containing liquid food (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, examples, examples of protein-containing food ingredients, examples of auxiliary ingredients, the amount of auxiliary ingredients in the food ingredients, and the definition, amount to be added, and method of addition (action time, action temperature, method of terminating the enzymatic reaction) of phospholipase D are the same as the definition, examples, examples of protein-containing food ingredients, examples of auxiliary ingredients, the amount of auxiliary ingredients in the food ingredients, and the definition, amount to be added, and method of addition (action time, action temperature, method of terminating the enzymatic reaction) of phospholipase D in the production method of the present invention.
• 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.
• Test Example 4 Confirmation of the Effect of Adding Phospholipase D to Beverages Using the blending recipes shown in Table 9 and following the sample preparation flow shown in FIG. 4, beverages Samples 4-1 and 4-2 were prepared. The resulting beverages, Samples 4-1 and 4-2, were subjected to a sensory evaluation by four expert panelists for smoothness and off-flavors/off-flavors according to the following evaluation criteria. The results are shown in Table 10.
• 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.
• Sample 5-4 which contained PLD and calcium chloride, showed improved smoothness compared to sample 5-1 (control).Sample 5-4 also showed improved smoothness compared to sample 5-3, which contained PLD but not calcium chloride.
• Sample 5-6 which contained PLD and calcined shell calcium, showed improved smoothness compared to Sample 5-1 (control).Sample 5-6 also showed improved smoothness compared to Sample 5-5, which contained PLD but no calcined shell calcium.
• Sample 5-8 to which PLD and glutathione-containing yeast extract were added, showed improved smoothness compared to Sample 5-1 (control).Sample 5-8 also showed improved smoothness compared to Sample 5-7, to which PLD was added but not glutathione-containing yeast extract was added.
• Sample 5-10 to which PLD and cysteine-containing yeast extract were added, showed improved smoothness compared to Sample 5-1 (control).Sample 5-10 also showed improved smoothness compared to Sample 5-9, to which PLD was added but no cysteine-containing yeast extract was added.
• Sample 5-12 to which PLD and cystine were added, showed improved smoothness compared to Sample 5-1 (control).Sample 5-12 also showed improved smoothness compared to Sample 5-11, to which PLD was added but no cystine was added.
• Sample 5-14 which contained PLD and calcium lactate, showed improved smoothness compared to Sample 5-1 (control).Sample 5-14 also showed improved smoothness compared to Sample 5-13, which contained PLD but not calcium lactate.
• Sample 5-16 which contained PLD and sodium carbonate, had improved smoothness compared to Sample 5-1 (control). Sample 5-16 also had improved smoothness compared to Sample 5-15, which contained PLD but no sodium carbonate.
• Sample 5-18 which contained PLD and trisodium phosphate, showed improved smoothness compared to sample 5-1 (control).Sample 5-18 also showed improved smoothness compared to sample 5-17, which contained PLD but no trisodium phosphate.
• Sample 5-20 to which PLD and iron-containing yeast were added, showed improved smoothness compared to sample 5-1 (control).Sample 5-20 also showed improved smoothness compared to sample 5-19, to which PLD was added but no iron-containing yeast was added.
• Sample 5-24 which contained PLD and glycine, showed improved smoothness compared to Sample 5-1 (control).Sample 5-24 also showed improved smoothness compared to Sample 5-23, which contained PLD but no glycine.
• Sample 5-26 which contained PLD and threonine, showed improved smoothness compared to Sample 5-1 (control).Sample 5-26 also showed improved smoothness compared to Sample 5-25, which contained PLD but no threonine.
• Sample 5-28 which contained PLD and manganese-containing yeast, had improved smoothness compared to sample 5-1 (control).Sample 5-28 also had improved smoothness compared to sample 5-27, which contained PLD but no manganese-containing yeast.
• Sample 5-30 which contained PLD and cysteine hydrochloride, showed improved smoothness compared to sample 5-1 (control).Sample 5-30 also showed improved smoothness compared to sample 5-29, which contained PLD but no cysteine hydrochloride.
• Sample 5-32 which contained PLD and alanine, showed improved smoothness compared to Sample 5-1 (control).Sample 5-32 also showed improved smoothness compared to Sample 5-31, which contained PLD but no alanine.
• Sample 5-34 which contained added PLD and cysteine, showed improved smoothness compared to Sample 5-1 (control).Sample 5-34 also showed improved smoothness compared to Sample 5-33, which contained added PLD but no added cysteine.
• Sample 5-36 to which PLD, sodium L-ascorbate, and ASO were added, showed improved smoothness compared to Sample 5-1 (control).
• Sample 5-36 also showed improved smoothness compared to Sample 5-2 (see Table 20), to which PLD was added but sodium L-ascorbate and ASO were not added.
• Sample 5-38 which contained PLD, glucose, and GO, showed improved smoothness compared to sample 5-1 (control).
• Sample 5-38 also showed improved smoothness compared to sample 5-2 (see Table 20), which contained PLD but no glucose or GO.
• Test Example 6 Confirmation of the Effect of Adding Phospholipase D to Plant-Based (PB) Beverages
• Samples 6-1 to 6-9 of PB beverages were prepared according to the blending recipes shown in Table 25 and the sample preparation flow shown in FIG.
• a sensory evaluation of smoothness was carried out by three expert panelists according to the following evaluation criteria. The results are shown in Table 26.
• samples 6-2 to 6-9 in which PLD was added to a PBP yogurt drink, had improved smoothness compared to sample 6-1 (control). Also, samples 6-3 to 6-9, in which PLD and auxiliary ingredients (threonine, manganese-containing yeast, glutathione-containing yeast extract, cysteine hydrochloride, glycine, alanine, or cysteine) were added to a PBP yogurt drink, had improved smoothness compared to sample 6-2, in which PLD was added but no auxiliary ingredients were added.
• Tables 28-1 and 28-2 show that samples 12-3 to 12-15, in which PLD was added in an amount that gave an enzyme activity of 0.00000065 to 6494.3 U per gram of protein in the sample, 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.
• 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.
• the present invention makes it possible to provide a protein-containing liquid food that improves the unpleasant texture that is derived from protein.

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