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
  • A23L2/52—Adding ingredients
  • A23L2/66—Proteins
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; PREPARATION THEREOF
  • 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
  • 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
  • A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
  • A23J1/14—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from leguminous or other vegetable seeds; from press-cake or oil-bearing seeds
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
  • A23J3/00—Working-up of proteins for foodstuffs
  • A23J3/14—Vegetable proteins
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
  • A23J3/00—Working-up of proteins for foodstuffs
  • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
  • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
  • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
  • A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L11/00—Pulses, i.e. fruits of leguminous plants, for production of food; Products from legumes; Preparation or treatment thereof
  • A23L11/30—Removing undesirable substances, e.g. bitter substances
  • A23L11/33—Removing undesirable substances, e.g. bitter substances using enzymes; Enzymatic transformation of pulses or legumes
• • 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
• • 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
  • A23L27/84—Flavour masking or reducing agents
• • 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
• • 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
  • A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
  • A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
  • A23L5/25—Removal of unwanted matter, e.g. deodorisation or detoxification using enzymes

Definitions

• the present invention relates to a method for producing a liquid composition containing processed hemp protein. Specifically, the present invention relates to a method for producing a processed hemp protein-containing liquid composition with improved solubility and suppressed change in taste.
• Vegetable protein drinks are gaining in popularity.
• Patent Document 1 discloses that by treating vegetable milk with protein deamidase, aggregation can be suppressed when added to hot liquid food or drink.
• the present inventors have attempted to improve the solubility of the plant milk by combining additional solubilizing means, but the solubility is still not improved, and in some cases, the additional solubilizing means is protein deamidase. Since they have different points of action, they undesirably change the component composition of the plant-based milk and even cause undesired changes in taste.
• the present invention improves the solubility of vegetable protein-containing liquid compositions such as vegetable milk (i.e., further increases the amount of protein dissolved in water than when solubilized by protein deamidase alone). ) and change in taste can be suppressed.
• the present inventors selected a hemp protein-containing liquid composition as a vegetable protein-containing liquid composition and treated it with a combination of bacterial-derived protease and protein deamidase to improve solubility and suppress changes in taste. I found what I could do. The present invention has been completed through further studies based on these findings.
• Section 1 A method for producing a processed hemp protein-containing liquid composition, comprising a step of treating a liquid composition containing hemp protein with a bacterial protease and a protein deamidating enzyme.
• Section 2. Item 2. The production method according to Item 1, wherein the bacterial protease is a protease derived from the genus Bacillus and/or Geobacillus.
• the bacterial protease is selected from the group consisting of Bacillus stearothermophilus, Bacillus licheniformis, Bacillus amyloliquefaciens and proteases derived from these Geobacillus genus. 3.
• Item 4 The production method according to any one of Items 1 to 3, wherein the liquid composition containing hemp protein is hemp milk.
• Item 5. A solubilizer for a hemp protein-containing liquid composition comprising a bacterial protease and a protein deamidating enzyme.
• Item 6. A solubilizer containing a bacterial protease and used for solubilizing a hemp protein-containing liquid composition treated with a protein deamidase while suppressing changes in taste.
• a processing technology that can improve the solubility of a hemp protein-containing liquid composition and suppress changes in taste.
• the method for producing a liquid composition containing processed hemp protein of the present invention is characterized by including a step of treating a liquid composition containing hemp protein with a bacterial protease and protein deamidase. and Hereinafter, the method for producing the processed hemp protein-containing liquid composition of the present invention will be described in detail.
• hemp protein-containing liquid composition used in the present invention is not particularly limited as long as it is a liquid in which hemp protein is dissolved and/or dispersed in water.
• Specific examples of the hemp protein-containing liquid composition include (i) a liquid obtained by dispersing a dry powder of a food material containing hemp protein in water; (ii) a food material containing hemp protein in water; Liquid obtained by crushing and dispersing, and optionally removing insoluble matter derived from skins of food materials by any means such as centrifugation, filtration, filter bag, sieve; (iii) above (i) or Liquid obtained by removing components other than hemp protein from the liquid of (ii) to increase the hemp protein content; (iv) Dry powder prepared from any of the liquids of (i) to (iii) above.
• hemp protein is dissolved and/or dispersed in water.
• a food material containing hemp protein is typically hemp seed.
• a preferred example of a liquid composition containing hemp protein is hemp milk.
• hemp in the present invention refers to so-called industrial hemp, and specifically refers to a variety that does not contain THC (tetrahydrocannabinol) or has a low THC concentration that causes perceptual alteration. Because industrial hemp does not contain THC or its low concentration, it has no efficacy as a sensory-altering drug and cannot lead to abuse.
• the protein content in the liquid composition containing hemp protein used in the present invention is not particularly limited, but is, for example, 0.1% by weight or more, preferably 0.5% by weight or more, more preferably 1% by weight or more, and 2% by weight. % or more, 3 wt% or more, 4 wt% or more, or 5 wt% or more.
• the upper limit of the protein content range in the liquid composition containing hemp protein is, for example, 11% by weight or less, preferably 10% by weight or less, more preferably 9% by weight, from the viewpoint of further improving the effect of suppressing change in taste. % by weight or less, more preferably 8% by weight or less, 7% by weight or less, and even more preferably 6% by weight or less.
• the protein deamidase used in the present invention is an enzyme that decomposes an amide group-containing side chain of a protein without cleaving peptide bonds or cross-linking the protein. is not particularly limited. In addition, as long as the above action is the main activity, it may further have the action of degrading the amide group-containing side chains of proteins, which accompanies cleavage of peptide bonds and cross-linking of proteins.
• protein deamidase examples include enzymes that deamidate glutamine residues in proteins and convert them to glutamic acid (e.g. protein glutaminase), and enzymes that deamidate asparagine residues in proteins and convert them to aspartic acid (e.g. protein asparaginase).
• protein deamidase examples include the genus Chryseobacterium, the genus Flavobacterium, the genus Empedobacter, the genus Sphingobacterium, the genus Aureobacterium ( Aureobacterium, Myroides, Luteimicrobium, Agromyces, Microbacterium, or Leifsonia.
• These protein deamidase enzymes are known, and for example, JP2000-50887A, JP2001-218590A, WO2006/075772A1, WO2015/133590, etc. can be referred to.
• One of these protein deamidase enzymes may be used alone, or two or more of them may be used in combination.
• protein deamidase is preferably derived from the genus Chryseobacterium, more preferably derived from the genus Chryseobacterium. more preferably from Chryseobacterium proteolyticum species, more preferably from Chryseobacterium proteolyticum strain 9670.
• the protein deamidase can be prepared from the culture solution of the microorganism from which the above protein deamidase is derived.
• a specific preparation method includes a method of recovering the protein deamidase from the culture solution or cells of the above microorganisms.
• the enzyme can be separated and/or purified after previously collecting the cells from the culture solution by filtration, centrifugation, or the like, if necessary.
• the cells were collected from the culture solution in advance, and then the cells were crushed by pressure treatment, ultrasonic treatment, or the like to expose the enzyme. The enzyme can then be isolated and/or purified.
• the enzyme separation and/or purification method known protein separation and/or purification methods can be used without particular limitation.
• Various chromatographic methods using The separated and/or purified enzyme can be pulverized by a drying method such as freeze-drying or vacuum drying, and pulverized using a suitable excipient and/or drying aid in the drying method.
• the separated and/or purified enzyme can be liquefied by adding appropriate additives and performing filtration sterilization.
• a commercial product can also be used as the protein deamidase, and a preferred example of a commercial product is protein glutaminase "Amano" 500 (derived from Chryseobacterium proteolyticum species) manufactured by Amano Enzyme Co., Ltd.
• the amount of protein deamidase used is not particularly limited, but the amount used per 1 g of hemp protein is, for example, 0.1 U or more. From the viewpoint of further enhancing the solubility-improving effect and/or the effect of suppressing changes in taste, the amount of protein deamidase used per 1 g of hemp protein is preferably 1 U or more, more preferably 2 U or more, and even more preferably 3 U or more. More preferably 4U or more, still more preferably 4.5U or more.
• the upper limit of the amount of protein deamidase to be used per gram of hemp protein is not particularly limited, but may be, for example, 50 U or less, 20 U or less, 10 U or less, 5.5 U or less, or 5 U or less.
• the amount of protein deamidase used per 1 g of hemp seed is, for example, 0.01 U or more.
• the amount of protein deamidase used per 1 g of hemp seed is preferably 0.1 U or more, 0.5 U or more, and more preferably 1 U or more. , more preferably 2 U or more, still more preferably 3 U or more, still more preferably 3.5 U or more.
• the upper limit of the amount of protein deamidase used per 1 g of hemp seed is not particularly limited, but examples thereof include 50 U or less, 20 U or less, 10 U or less, 5 U or less, or 4 U or less.
• 1 unit (1 U) is defined as the amount of enzyme that liberates 1 ⁇ mol of ammonia per minute using benzyloxycarbonyl-L-glutaminylglycine (Z-Gln-Gly) as a substrate.
• Bacterial Protease The bacterial protease used in the present invention is not particularly limited as long as it is an enzyme derived from bacteria that hydrolyzes peptide bonds of proteins. The bacterial protease further enhances the effect of protein deamidase on improving solubility and suppresses changes in taste.
• the bacterial-derived protease is not particularly limited, but from the viewpoint of further enhancing the solubility-enhancing effect and/or the taste-change-suppressing effect, proteases derived from the genus Bacillus and/or Geobacillus are preferred, and more preferably Bacillus. Bacillus stearothermophilus, Bacillus licheniformis, Bacillus amyloliquefaciens, Bacillus subtilis and proteases derived from these Geobacillus species.
• one of these proteases may be used, or two or more may be used in combination.
• these bacterial-derived proteases Geobacillus stearothermophilus, Bacillus licheniformis, and Bacillus amyloliquefaciens are more preferable from the viewpoint of further enhancing the solubility-improving effect and/or the effect of suppressing change in taste. be done.
• a bacterial protease can be prepared by a known method.
• it when preparing a protease derived from the genus Bacillus, it can be easily prepared by culturing a bacterium belonging to the genus Bacillus and isolating the protease using a known means, a method using genetic recombination technology, or the like.
• you may use a commercial item as a bacterial-derived protease.
• bacterial-derived proteases include Samoase PC10F (Geobacillus stearothermophilus-derived neutral protease), Protin SD-NY10 (Bacillus amyloliquefaciens-derived neutral protease), manufactured by Amano Enzyme Co., Ltd. Protin SD-AY10 (Bacillus licheniformis-derived alkaline protease), Protease N "Amano" G (Bacillus subtilis-derived neutral protease), Neutrase (Bacillus amyloliquefaciens-derived) manufactured by Novozymes Japan Co., Ltd.
• Neutral protease Esperase (Bacillus sp.-derived alkaline protease), Savinase (Bacillus sp.-derived alkaline protease), Evalase (Bacillus sp.-derived alkaline protease), Alcalase (Bacillus licheniformis-derived alkaline protease); Yakult Pharmaceutical Industry Co., Ltd. and Alloase NS (Bacillus subtilis-derived neutral protease), Alloase AP-10 (Bacillus subtilis-derived neutral protease), Alloase NP-10 (Bacillus subtilis-derived neutral protease), etc., manufactured by Epson.
• the amount of bacterial protease used is not particularly limited, but the amount used per 1 g of hemp protein is, for example, 0.1 U or more. From the viewpoint of further enhancing the solubility-improving effect, the amount of bacterial protease used per 1 g of hemp protein is preferably 1 U or more, more preferably 10 U or more, still more preferably 100 U or more, still more preferably 200 U or more, and even more preferably. 300U or more can be mentioned.
• the upper limit of the amount of the bacterial protease used per 1 g of hemp protein is not particularly limited, but from the viewpoint of further enhancing the effect of suppressing change in taste, it is preferably 1000 U or less, more preferably 800 U or less, 700 U or less, and even more preferably 700 U or less. 600 U or less, more preferably 500 U or less.
• the amount of bacterial protease used per 1 g of hemp seed is, for example, 0.1 U or more.
• the amount of bacterial protease used per 1 g of hemp seeds is preferably 1 U or more, more preferably 10 U or more, and even more preferably 100 U or more, and the use of bacterial protease per 1 g of hemp seeds.
• the upper limit of the amount range is not particularly limited, it is preferably 1000 U or less, more preferably 600 U or less, 500 U or less, still more preferably 400 U or less, and still more preferably 350 U or less from the viewpoint of further enhancing the effect of suppressing change in taste. be done.
• the ratio of the protein deamidating enzyme and the bacterial protease to be used is determined based on the amount of each enzyme used.
• the amount is preferably 1 U or more, more preferably 10 U or more, 20 U or more, still more preferably 30 U or more, 40 U or more, still more preferably 50 U or more, and even more preferably 60 U or more.
• the upper limit of the amount of the bacterial protease per 1 U of protein deamidase is preferably 200 U or less, more preferably 150 U or less, 120 U or less, and even more preferably 100 U or less, from the viewpoint of further enhancing the effect of suppressing change in taste. are mentioned.
• the protease activity shall be measured by the Folin method using casein as a substrate. That is, the activity of protease is defined as 1 unit (1U) of the amount of enzyme that causes an increase in Folin's test solution coloring substance equivalent to 1 ⁇ g of tyrosine per minute in an enzymatic reaction using casein as a substrate in a conventional manner.
• the order in which the bacterial-derived protease and the protein deamidating enzyme are allowed to act is not particularly limited, and the order of each enzyme is arbitrary. may be caused to act sequentially, or both enzymes may be caused to act simultaneously.
• the treatment temperature with the bacterial protease and the protein deamidase is not particularly limited, and can be appropriately determined by those skilled in the art depending on the optimum temperature of the enzyme used and/or the thermal properties of the hemp protein-containing liquid composition. , for example, 40 to 70°C, preferably 48 to 62°C.
• the enzymatic treatment reaction time of the hemp protein-containing liquid composition is not particularly limited, and may be appropriately determined according to the preparation scale of the composition, the timing of addition of the enzyme, etc. For example, 30 minutes or longer, preferably 50 minutes or longer. are mentioned.
• the upper limit of the enzymatic treatment reaction time range is not particularly limited, but includes, for example, 12 hours or less, 8 hours or less, or 4 hours or less.
• the hemp protein-containing liquid composition is subjected to enzyme deactivation treatment, then cooled, and subjected to post-treatment such as filtration as necessary to obtain a processed hemp protein-containing liquid composition.
• the resulting processed hemp protein-containing liquid composition can also be prepared as a solid hemp protein composition having improved solubility in water while suppressing change in taste through a drying process.
• the method of drying is not particularly limited, and examples thereof include freeze drying, vacuum drying, spray drying and the like.
• the solid hemp protein composition may also be in the form of powder, granules, granules, and the like.
• the present invention also provides a solubilizer for a hemp protein-containing liquid composition comprising a bacterial-derived protease and a protein deamidase.
• solubilizer the types and amounts of ingredients used are as shown in the above "1. Method for producing liquid composition containing processed hemp protein”.
• Solubilizer for Hemp Protein-Containing Liquid Composition Treated with Protein Deamidase suppresses changes in the taste of the hemp protein-containing liquid composition treated with protein deamidase.
• the present invention also provides a solubilizer that contains a bacterial protease and is used to solubilize a hemp protein-containing liquid composition that is treated with a protein deamidase while suppressing changes in taste.
• solubilizing agent means solubilization that further increases the amount of protein dissolved in water as compared to the case where protein is solubilized only by protein deamidase.
• specific usage modes of this solubilizer include a mode in which the hemp protein-containing liquid composition is treated using the solubilizer and protein deamidase at the same time, and a mode in which the hemp protein-containing liquid composition is treated with protein deamidase. and an embodiment in which the hemp protein-containing liquid composition is treated with a solubilizer and then treated with a protein deamidase.
• solubilizer the types and amounts of ingredients used are as shown in the above "1. Method for producing liquid composition containing processed hemp protein”.
• the amount of enzyme that causes an increase in Folin's test solution coloring substance equivalent to 1 ⁇ g of tyrosine per minute was defined as 1 unit (1 U).
• Protein deamidase activity value measurement method 0.1 mL of a 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 temperature was adjusted to 37°C. After standing for 10 minutes, 1 mL of 0.4 M TCA solution was added to stop the reaction. As a blank, 1 mL of 0.4 M TCA test solution was added to 1 mL of 0.2 M phosphate buffer (pH 6.5) containing 30 mM Z-Gln-Gly, and 0.1 mL of sample solution containing protein deamidase was added, It was left at 37°C for 10 minutes.
• ammonia test Wako Flujifilm Wako Pure Chemical
• the ammonia concentration in the reaction solution was obtained from a calibration curve representing the relationship between ammonia concentration and absorbance (630 nm) prepared using an ammonia standard solution (ammonium chloride).
• the activity of protein deamidase was calculated from the following formula, with the amount of enzyme that generates 1 ⁇ mol of ammonia per minute as 1 unit (1 U).
• the reaction liquid 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.
• hemp milk can be produced while suppressing changes in taste compared to the case where protein deamidase is used alone. It was possible to increase the protein solubility of milk (Examples 1-11). Further, as is clear from the comparison between Comparative Examples 18, 20, 21, 23, and 25 and Examples 1 to 6 and the comparison between Comparative Example 13 and Examples 7 to 9, while suppressing the change in taste, It was shown that the effect of increasing the protein solubility of hemp milk is a unique effect of selecting hemp milk as the vegetable milk and bacterial protease as the protease.

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• 2022
  • 2022-04-05 EP EP22784670.6A patent/EP4321032A4/en active Pending
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  • 2022-04-05 WO PCT/JP2022/017087 patent/WO2022215688A1/ja not_active Ceased
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