Classifications

• • 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
  • A23L2/38—Other non-alcoholic beverages
• • 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
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
  • A23J3/00—Working-up of proteins for foodstuffs
  • A23J3/14—Vegetable proteins
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • 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
  • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
  • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
  • A23L33/17—Amino acids, peptides or proteins
  • A23L33/185—Vegetable proteins
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
  • C12P21/00—Preparation of peptides or proteins
  • C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
• • C—CHEMISTRY; METALLURGY
  • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
  • C12Y—ENZYMES
  • C12Y305/00—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5)
  • C12Y305/01—Hydrolases acting on carbon-nitrogen bonds, other than peptide bonds (3.5) in linear amides (3.5.1)
  • C12Y305/01002—Glutaminase (3.5.1.2)

Definitions

• the present invention relates to a processing technology that improves the foaming properties of an oat protein-containing liquid composition.
• Patent Document 1 describes how treating oat suspension with ⁇ -amylase and ⁇ -amylase can solve the high viscosity problem inherent to oat suspension while preserving protein and ⁇ -glucan.
• Patent Document 2 describes how the dispersion stability and solubility of plant-based milk can be improved by treating it with protein deamidating enzymes.
• oats are known as a highly nutritious food ingredient.
• oat milk is treated with protein deamidase, a modification effect that improves foaming properties is obtained.
• the foaming property improvement effect that can be obtained by simply treating with protein deamidase is not sufficient, and it is desirable to be able to further improve this modification effect.
• the present invention aims to provide a processing technology that improves the foaming properties of oat protein-containing liquid compositions.
• Item 1 An enzyme treatment step of allowing a protein deamidating enzyme to act on an oat protein-containing liquid composition at a predetermined pH to obtain an enzyme-treated liquid composition;
• a method for producing a processed oat protein-containing liquid composition comprising: a pH reducing step of reducing the pH of the enzyme-treated liquid composition to obtain a processed oat protein-containing liquid composition.
• Item 2. The method according to Item 1, wherein the pH of the processed oat protein-containing liquid composition at 25° C. is 0.2 to 4, calculated by subtracting the pH of the processed oat protein-containing liquid composition at 25° C. from the predetermined pH at 25° C.
• the present invention provides a processing technology that improves the foaming properties of an oat protein-containing liquid composition.
• Method for producing a processed auto protein-containing liquid composition is characterized by comprising an enzyme treatment step in which a protein deamidating enzyme is applied to an auto protein-containing liquid composition at a predetermined pH to obtain an enzyme-treated liquid composition, and a pH reduction step in which the pH of the enzyme-treated liquid composition is reduced to obtain a processed auto protein-containing liquid composition.
• the processed auto protein-containing liquid composition obtained by the production method of the present invention is processed to improve foamability compared to the case where the pH reduction step is not performed.
• the foam stability of the auto protein-containing liquid composition is reduced by treating it with protein deamidating enzyme
• the preferred form of the processed auto protein-containing liquid composition obtained by the production method of the present invention is also processed to improve foam stability compared to the case where the pH reduction step is not performed.
• the production method of the processed auto protein-containing liquid composition of the present invention will be described in detail below.
• protein deamidating enzyme is allowed to act on the autoprotein-containing liquid composition at a predetermined pH to obtain an enzyme-treated liquid composition.
• an autoprotein-enzyme mixture containing the autoprotein-containing liquid composition and protein deamidating enzyme at the predetermined pH is prepared, and an enzyme reaction is allowed to proceed to obtain the enzyme-treated liquid composition.
• Oat protein-containing liquid composition The oat protein-containing liquid composition is not particularly limited as long as it is a liquid in which oat protein is dissolved and/or dispersed in water.
• oat protein-containing liquid compositions include: (i) a liquid obtained by dispersing a dry powder (preferably oat flour) of an oat protein-containing material (preferably oat seeds, more preferably hulled oats) in water, and removing insoluble matter derived from the bran layer of the oat seeds, etc., as necessary, by any means such as centrifugal filtration, filtration, a filter bag, or a sieve; (ii) a liquid obtained by crushing and dispersing an oat protein-containing material (preferably oat seeds, more preferably hulled oats) in water, and removing insoluble matter derived from the bran layer of the oat seeds, etc., as necessary, by any means such as centrifugal filtration, filtration, filtration, filtration
• the oat protein content in the oat protein-containing liquid composition used in the present invention is not particularly limited, but may be, for example, 0.01 to 15 wt%, 0.1 to 7.5 wt%, or 0.25 to 5 wt%, and from the viewpoint of further increasing the foamability of the processed oat protein-containing liquid composition, or from the viewpoint of improving the foam stability in addition to the above, the content is preferably 0.5 to 3 wt%, or 0.75 to 2.5 wt%, and more preferably 1 to 2 wt%, 1.2 to 1.8 wt%, or 1.4 to 1.6 wt%.
• the oat protein-containing liquid composition may or may not contain any other ingredients in addition to the oat protein and water.
• Other ingredients include ingredients derived from oat seeds, other food ingredients, and food additives.
• Food additives include thickeners, binders, seasonings, pH adjusters, buffers, colorants, fragrances, etc.
• Protein deamidating enzymes are not particularly limited in type, origin, etc., as long as they are enzymes that degrade amide group-containing side chains of proteins without cleaving peptide bonds or crosslinking proteins.
• Examples of protein deamidating enzymes include those of the genus Chryseobacterium , Flavobacterium, Empedobacter, Sphingobacterium, etc., disclosed in JP-A-2000-50887, JP-A-2001-218590, and WO 2006/075772, and those of the genus Chryseobacterium, Flavobacterium, Empedobacter, Sphingobacterium, etc., disclosed in JP-A-2000-50887, JP-A-2001-218590, and WO 2006/075772, and those of the genus Sphingobacterium, etc., disclosed in JP-A-2000-2 ...
• Examples of protein deamidases that can be used include those derived from the genera Bacillus subtilis, ...
• protein deamidating enzymes examples include protein glutaminase and protein asparaginase, and in a broader sense, also protein arginine deiminase.
• protein glutaminase is preferred.
• protein deamidating enzymes derived from the genus Chryseobacterium are more preferred, protein glutaminases derived from the genus Chryseobacterium are even more preferred, and protein glutaminase derived from the species Chryseobacterium proteolyticum is even more preferred.
• Protein deamidase can be prepared from the culture medium of the microorganism from which the protein deamidase is derived. Specific preparation methods include a method of recovering protein deamidase from the culture medium or cells of the microorganism. For example, when a protein deamidase-secreting microorganism is used, the cells can be recovered from the culture medium in advance by filtration, centrifugation, or the like as necessary, and the enzyme can be separated and/or purified. When a protein deamidase-nonsecreting microorganism is used, the cells can be recovered from the culture medium in advance by pressure treatment, ultrasonic treatment, or the like to expose the enzyme, and the enzyme can be separated and/or purified.
• a known protein separation and/or purification method can be used without any particular limitation, and examples of the method include centrifugation, UF concentration, salting out, various chromatography methods using ion exchange resins, and the like.
• the separated and/or purified enzyme can be powdered by a drying method such as freeze-drying or vacuum drying, and can also be powdered using an appropriate excipient and/or drying aid in the drying method. Additionally, the isolated and/or purified enzymes can be liquefied by adding appropriate additives and sterilizing by filtration.
• the amount of protein deamidating enzyme used in the oat protein-containing liquid composition is not particularly limited, but may be, for example, 0.05 U or more, 0.1 U or more, or 0.5 U or more per gram of oat protein contained in the oat protein-containing liquid composition. From the viewpoint of further increasing the foamability of the processed oat protein-containing liquid composition, or from the viewpoint of improving foam stability in addition to the above viewpoint, the amount is preferably 1 U or more, 1.5 U or more, 2 U or more, or 2.5 U or more, more preferably 3 U or more, 3.5 U or more, or 4 U or more, and even more preferably 4.5 U or more, or 5 U or more.
• the upper limit of the amount used per gram of oat protein contained in the oat protein-containing liquid composition is not particularly limited, but may be, for example, 500 U or less, 200 U or less, 100 U or less, 80 U or less, 60 U or less, 40 U or less, 30 U or less, 20 U or less, 12 U or less, 8 U or less, or 7 U or less.
• the amount of enzyme that liberates 1 ⁇ mol of ammonia per minute using benzyloxycarbonyl-L-glutaminylglycine (Z-Gln-Gly) as a substrate is defined as 1 unit (1 U).
• the method for preparing the autoprotein-enzyme mixture is not particularly limited. For example, there may be mentioned a method of preparing an autoprotein-containing liquid composition and mixing the autoprotein-containing liquid composition with protein deamidating enzyme to prepare the autoprotein-enzyme mixture; and a method of preparing the autoprotein-containing liquid composition and the autoprotein-enzyme mixture simultaneously by mixing the materials of the autoprotein-containing liquid composition with protein deamidating enzyme.
• the specific range of the predetermined pH is not particularly limited as long as the effects of the present invention can be obtained, and can be appropriately set according to the optimal pH of the protein deamidating enzyme used.
• Specific examples of the predetermined pH include, for example, 5.0 to 9.0 or 5.0 to 8.5.
• the predetermined pH is preferably 5.5 to 8.5, more preferably 6 to 8.4, even more preferably 6.5 to 8.3, even more preferably 7 to 8.2, and even more preferably 7.2 to 8.2, 7.4 to 8.2, 7.6 to 8.2, or 7.8 to 8.2.
• processing conditions for the autoprotein-enzyme mixture are not particularly limited as long as the effects of the present invention can be obtained.
• the treatment temperature can be set appropriately depending on the optimum temperature of the protein deamidation enzyme used.
• Specific examples of the treatment temperature include, for example, 20 to 70°C, preferably 40 to 68°C, more preferably 50 to 66°C, even more preferably 55 to 64°C, and even more preferably 58 to 62°C.
• the treatment time can be set appropriately depending on the scale of the autoprotein-enzyme mixture and the treatment temperature, etc.
• Specific examples of the treatment time include, for example, 0.5 to 4 hours, preferably 0.6 to 2 hours, more preferably 0.7 to 1.5 hours, or 0.8 to 1.2 hours.
• processing conditions may be determined through preliminary experiments depending on the desired foaming property, or the degree of foaming property and foam stability, of the processed oat protein-containing liquid composition.
• pH Lowering Step the pH of the enzyme-treated liquid composition obtained in the above enzyme treatment step is lowered to obtain a liquid composition containing processed oat proteins.
• Methods for lowering the pH include adding a pH adjuster, mixing with an acidic food or beverage, and adding an acidic food additive other than a pH adjuster.
• a method for lowering the pH any of these methods may be used alone, or two or more methods may be used in combination.
• pH adjusters include inorganic acids such as hydrochloric acid and sulfuric acid; organic acids such as lactic acid and citric acid; and salts of strong acids and weak bases.
• inorganic bases such as hydroxides of alkali metals (sodium hydroxide, potassium hydroxide, etc.); and organic bases such as triethanolamine and triisopropanolamine may be used in combination to finely adjust the pH.
• inorganic acids are preferable.
• Examples of acidic food or beverage include oat yogurt, coffee, and fruit drinks. Examples of these acidic food or beverage include unheated and uncooled food or beverage, or cooled (for example, above 5°C but below room temperature or below 5°C). Examples of acidic food additives other than pH adjusters include acidic amino acids and acidic vitamins. These pH adjusters, acidic foods and beverages, and food additives may each be used alone or in combination.
• the degree to which the pH is lowered may be appropriately set depending on the desired degree of foamability or the degree of foamability and foam stability of the processed oat protein-containing liquid composition, but examples of the degree to which the value obtained by subtracting the pH of the processed oat protein-containing liquid composition at 25°C from the above-mentioned predetermined pH at 25°C is 0.2 to 4, for example.
• the degree of lowering the pH is preferably 1 to 4, more preferably 1.5 to 4, even more preferably 2 to 4, even more preferably 2.4 to 4, 2.6 to 3.5, or 2.8 to 3.2.
• the pH at 25°C of the processed oat protein-containing liquid composition obtained in the pH lowering step is specifically, for example, 4 to 7.8, and from the viewpoint of further increasing the foamability of the processed oat protein-containing liquid composition, or from the viewpoint of improving foam stability in addition to the above viewpoint, it is preferably 4 to 7.5 or 4 to 7, more preferably 4 to 6.6, even more preferably 4 to 6.1, and even more preferably 4 to 5.6.
• foamability and foam stability are significantly deteriorated at low pH, but the processed oat protein-containing liquid composition obtained by the present invention has excellent foamability, or excellent foamability and foam stability, so that excellent foamability, or excellent foamability and foam stability can be obtained even at a low pH.
• pH values at 25°C for the processed oat protein-containing liquid composition include 4 to 6.6, more preferably 4 to 6.1, even more preferably 4 to 5.6, and even more preferably 4 to 5.4, 4.5 to 5.4, 4.5 to 5.2, 4.8 to 5.2, or 4.8 to 5.
• the method for producing a processed oat protein-containing liquid composition of the present invention may or may not include other steps in addition to the above-mentioned enzyme treatment step and pH lowering step.
• Examples of other steps include a step of preparing an oat protein-containing liquid composition, a step of inactivating an enzyme, a step of enzyme treatment with an enzyme other than protein deamidating enzyme, a cooling step, a filtration step, a drying step, etc. These other steps may be performed individually or in combination of two or more steps.
• the preparation step of the oat protein-containing liquid composition can be carried out by any method capable of preparing an oat protein-containing liquid composition.
• a method of preparing the composition by dispersing a dry powder (preferably oat flour) of a material containing oat protein (preferably oat seeds, more preferably hulled oats) in water, and removing insoluble matter derived from the bran layer of the oat seeds, etc., as necessary, by any means such as centrifugal filtration, filtration, a filter bag, a sieve, etc.;
• a method of preparing the composition by crushing and dispersing a material containing oat protein (preferably oat seeds, more preferably hulled oats) in water, and removing insoluble matter derived from the bran layer of the oat seeds, etc., as necessary, by any means such as centrifugal filtration, filtration, a filter bag, a sieve, etc.;
• III a method of
• the liquid obtained by any of the above methods (I) to (IV) is treated with amylase.
• amylase include ⁇ -amylase and ⁇ -amylase. Either one of these amylases may be used alone, or both may be used in combination.
• the oat protein-containing liquid composition is treated with ⁇ -amylase and ⁇ -amylase.
• the ⁇ -amylase is not particularly limited, but examples thereof include ⁇ -amylases derived from the genus Aspergillus (e.g., Aspergillus oryzae, Aspergillus niga, etc.) and the genus Bacillus (e.g., Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, etc.), preferably ⁇ -amylases derived from the genus Bacillus, and more preferably ⁇ -amylases derived from the species Bacillus amyloliquefaciens.
• Aspergillus e.g., Aspergillus oryzae, Aspergillus niga, etc.
• Bacillus e.g., Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus licheniformis, etc.
• ⁇ -amylases derived from the genus Bacillus e.
• the amount of ⁇ -amylase used is, for example, 0.01 to 1000 U, preferably 0.1 to 100 U, more preferably 0.5 to 50 U, even more preferably 1 to 30 U, and even more preferably 5 to 20 U or 8 to 15 U per gram of starch in the oat protein-containing liquid composition.
• potato starch is used as a substrate, and the amount of enzyme that reduces the color produced by iodine by 10% in one minute is defined as one unit (1U).
• the ⁇ -amylase is not particularly limited, but examples thereof include ⁇ -amylase derived from plants (wheat, soybean, etc.) and Bacillus genus.
• ⁇ -amylase derived from the Bacillus genus is used, and more preferably, ⁇ -amylase derived from the Bacillus flexus species is used.
• the amount of ⁇ -amylase used is, for example, 0.0001 to 9 U, preferably 0.001 to 0.9 U, more preferably 0.01 to 0.4 U, even more preferably 0.03 to 0.2 U, and even more preferably 0.06 to 0.12 U per gram of starch in the oat protein-containing liquid composition.
• the amount of enzyme that increases the reducing power equivalent to 1 mg of glucose per minute using potato starch as a substrate is defined as 1 unit (1 U).
• treatment pH treatment pH
• treatment temperature treatment time
• treatment time treatment pH, treatment temperature, treatment time
• the conditions for amylase treatment may be appropriately set depending on the optimum pH and temperature of the enzyme used, the scale of the autoprotein-containing liquid composition, the desired degree of solubility, etc.
• the treatment pH is, for example, 5.5 to 7.5 as the pH (25°C) of the oat protein-containing liquid composition before amylase treatment, and from the viewpoint of further increasing foamability, it is preferably 6.2 to 7.2, more preferably 6.5 to 7.2, even more preferably 6.8 to 7.2, and particularly preferably 7.0, and from the viewpoint of further increasing foam stability, it is preferably 6.2 to 7.2, more preferably 6.3 to 6.7, and particularly preferably 6.5.
• the treatment temperature is, for example, 50 to 65°C, preferably 50 to 60°C, and more preferably 52 to 56°C.
• the treatment time is, for example, 0.5 to 2 hours.
• the temperature and/or pH conditions for inactivating the enzyme used can be appropriately selected taking into consideration the temperature and/or pH characteristics of the processed oat protein-containing liquid composition, and preferably the temperature conditions can be selected.
• Specific temperature conditions include, for example, 85 to 120°C, preferably 90 to 100°C, and more preferably 93 to 98°C, and the treatment time can be, for example, 1 to 30 minutes, or 1 to 10 minutes, and preferably 3 to 8 minutes.
• the liquid composition containing processed oat protein obtained by the above-mentioned manufacturing method can be used as an ingredient for food and drink (food and drink containing oat protein). Since the liquid composition containing processed oat protein has excellent foaming properties, or foaming properties and foam stability, the specific form of the food and drink containing oat protein can be a food and drink in which the liquid composition containing processed oat protein is foamed, or a food and drink that is foamed when used and consumed.
• oat protein-containing foods and beverages include oat milk, oat cream, oat yogurt, and foods and beverages containing these. These foods and beverages may be mixed with other beverages such as tea, coffee, and fruit drinks, or may be mixed with other beverages when used.
• suitable forms of these foods and beverages include those prepared as oat yogurt; those mixed with low pH beverages such as coffee and fruit drinks; and those mixed with low pH beverages when used.
• the temperature of the foods and beverages is not particularly limited, and may be any of heated foods and beverages (e.g., above room temperature but below 50°C, or above 50°C), unheated and uncooled foods and beverages, and cooled foods and beverages (e.g., above 5°C but below room temperature, or below 5°C).
• Such foods and beverages can be produced using the above-mentioned processed oat protein-containing liquid composition, as appropriate, through a seasoning step and/or a cooking step.
• the specific methods used in the seasoning step and cooking step can be appropriately determined by those skilled in the art depending on the final form of the food and beverage.
• B. Enzyme Activity Measurement Method [B-1. Protein deamidation enzyme] The protein deamidase activity was measured by the following method. 0.1 mL of the sample solution containing protein deamidase was added to 1 mL of 0.2 M phosphate buffer (pH 6.5) containing 30 mM Z-Gln-Gly, and the mixture was left at 37° C. for 10 minutes, after which 1 mL of 0.4 M TCA solution was added to stop the reaction.
• the amount of ammonia produced in the reaction solution was measured using an Ammonia Test Wako (FUJIFILM Wako Pure Chemical Corporation).
• the ammonia concentration in the reaction solution was calculated from a calibration curve showing the relationship between ammonia concentration and absorbance (630 nm) created using an ammonia standard solution (ammonium chloride).
• the activity of protein deamidating enzyme was calculated from the following formula, with 1 unit (1U) being the amount of enzyme that produces 1 ⁇ mol of ammonia per minute.
• the reaction solution volume is 2.1
• the enzyme solution volume is 0.1
• Df is the dilution ratio of the enzyme solution.
• 17.03 is the molecular weight of ammonia.
• [B-2. ⁇ -Amylase] The ⁇ -amylase activity was measured by the following method. 10 mL of 1% potato starch substrate solution (0.1 mol/L acetic acid (pH 5.0)) was heated at 37°C for 10 minutes, after which 1 mL of sample solution containing ⁇ -amylase was added and immediately shaken. This solution was left to stand at 37°C for 10 minutes, after which 1 mL of this solution was added to 10 mL of 0.1 mol/L hydrochloric acid solution and immediately shaken.
• 1% potato starch substrate solution 0.1 mol/L acetic acid (pH 5.0)
• ⁇ -amylase activity was measured by the following method. Potato starch was used as the substrate, and was dried at 105°C for 2 hours. 1.0 g of the dried material was weighed out, 20 mL of water was added, and 5 mL of sodium hydroxide solution (2 mol/L) was gradually added while stirring to form a paste. Next, the mixture was heated in a boiling water bath for 3 minutes while stirring, and then 25 mL of water was added.
• hydrochloric acid solution (2 mol/L) and hydrochloric acid solution (0.1 mol/L) were added to neutralize, 10 mL of 1 mol/L acetic acid/sodium acetate buffer (pH 5.0) was added, and water was added to make 100 mL to prepare the substrate solution.
• a comparison solution was prepared in the same manner as the test solution, using 10 mL of water instead of the substrate solution.
• the liberated iodine in the test solution and comparison solution was titrated with 0.05 mol/L sodium thiosulfate solution.
• the end point was determined when 1-2 drops of soluble starch solution were added as the titration approached the end point, and the resulting blue color disappeared.
• the amount of enzyme that brings about an increase in reducing power equivalent to 1 mg of glucose per minute was defined as 1 unit (1 U), and was calculated using the following formula.
• oat protein-containing liquid composition An oat protein-containing liquid composition was prepared as follows. 18.1 g of oat flour was mixed with 150 g of water to prepare a suspension in a 200 mL Erlenmeyer flask. The pH (25°C) of this suspension was adjusted to 6.5, 7.0, or 7.5, and 10 U of ⁇ -amylase per 1 g of starch and 0.09 U of ⁇ -amylase per 1 g of starch were added and reacted at 54°C for 1 hour. Thus, an oat protein-containing liquid composition (oat milk) was obtained.
• Protein deamidating enzyme was added to the obtained autoprotein-containing liquid composition at a rate of 5 U per gram of protein, and the pH was adjusted to 8.0 (25°C), after which the mixture was reacted at 60°C for 1 hour. After the reaction, the mixture was heated at 95°C for 5 minutes to inactivate the enzyme. The mixture was then centrifuged at 1,000 rpm for 1 minute, and the supernatant (enzyme-treated liquid composition) was collected.
• the pH (25°C) of the collected supernatant (enzyme-treated liquid composition) was adjusted to 5.0, 5.5, 6.0, 6.5, 7.0, 7.5, or 8.0 to prepare a processed oat protein-containing liquid composition (processed oat milk).
• a processed oat protein-containing liquid composition processed oat milk.
• High-concentration aqueous NaOH and HCl solutions were used as pH adjusters, so there was almost no increase in the liquid volume due to the pH adjustment.
• a liquid composition containing oat protein that was not treated with protein deamidase (PG) was prepared by carrying out the same procedure, except that the enzyme treatment with protein deamidase (PG) was not carried out.
• foaming improvement index 1 in Tables 2A and 2B the foaming properties of the processed oat milk (Examples 1 to 6) improved when the pH was lowered after PG treatment. Furthermore, as shown in Table 2A, when the pH was lowered to 5.0, the foaming properties significantly deteriorated (Comparative Example 7), but as shown by foaming improvement index 2 in Table 2B, the processed oat milk exhibited excellent foaming properties even when the pH was lowered to 5.0 after PG treatment (Example 6).
• the foaming property of the processed oat milk was improved by lowering the pH after PG treatment.
• the foam stability of processed oat milk was reduced by PG treatment (Comparative Example 8), but the foam stability was improved by lowering the pH after PG treatment (Examples 1 to 6).
• the degree of improvement in foam stability was equal to or greater than that of untreated PG when the pH was lowered to 6.5 or less (Examples 3 to 6).
• foam stability deteriorates when the pH is lowered to 5.0 (Comparative Example 7), but as shown by foam stability improvement index 2 in Table 5B, processed oat milk exhibited excellent foam stability even when the pH was lowered to 5.0 after PG treatment, and the degree of improvement exceeded that of untreated PG (Example 6).
• the foam stability of processed oat milk decreases with PG treatment (Comparative Example 14), but the foam stability improves when the pH is lowered after PG treatment (Examples 8-10, 15), and the degree of improvement in foam stability is equal to or greater than that of untreated PG when the pH is lowered to 6.5 or lower (Examples 9, 10, 15).

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