US20170318841A1 - Liquid oat base - Google Patents
Liquid oat base Download PDFInfo
- Publication number
- US20170318841A1 US20170318841A1 US15/656,259 US201715656259A US2017318841A1 US 20170318841 A1 US20170318841 A1 US 20170318841A1 US 201715656259 A US201715656259 A US 201715656259A US 2017318841 A1 US2017318841 A1 US 2017318841A1
- Authority
- US
- United States
- Prior art keywords
- protein
- oat
- oats
- amylase
- steamed
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 239000007788 liquid Substances 0.000 title claims abstract description 14
- 235000007319 Avena orientalis Nutrition 0.000 claims abstract description 94
- 244000075850 Avena orientalis Species 0.000 claims abstract description 82
- 239000000463 material Substances 0.000 claims abstract description 14
- 238000004519 manufacturing process Methods 0.000 claims abstract description 8
- 241000209761 Avena Species 0.000 claims abstract 12
- 230000003381 solubilizing effect Effects 0.000 claims abstract 2
- 238000000034 method Methods 0.000 claims description 50
- 230000008569 process Effects 0.000 claims description 41
- 102000004169 proteins and genes Human genes 0.000 claims description 36
- 108090000623 proteins and genes Proteins 0.000 claims description 36
- 108010065511 Amylases Proteins 0.000 claims description 18
- 102000013142 Amylases Human genes 0.000 claims description 18
- 235000019418 amylase Nutrition 0.000 claims description 18
- 229920002472 Starch Polymers 0.000 claims description 17
- 235000019698 starch Nutrition 0.000 claims description 17
- 239000008107 starch Substances 0.000 claims description 17
- 239000004382 Amylase Substances 0.000 claims description 15
- 108091005804 Peptidases Proteins 0.000 claims description 13
- 101001122938 Homo sapiens Lysosomal protective protein Proteins 0.000 claims description 9
- 102100028524 Lysosomal protective protein Human genes 0.000 claims description 9
- 239000004365 Protease Substances 0.000 claims description 8
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 8
- 239000007858 starting material Substances 0.000 claims description 8
- VTYYLEPIZMXCLO-UHFFFAOYSA-L Calcium carbonate Chemical compound [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 claims description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 6
- 238000007792 addition Methods 0.000 claims description 6
- 108010019077 beta-Amylase Proteins 0.000 claims description 6
- 235000013312 flour Nutrition 0.000 claims description 6
- 235000013305 food Nutrition 0.000 claims description 6
- 102000009127 Glutaminase Human genes 0.000 claims description 5
- 108010073324 Glutaminase Proteins 0.000 claims description 5
- 239000001506 calcium phosphate Substances 0.000 claims description 5
- 230000015556 catabolic process Effects 0.000 claims description 5
- 238000006731 degradation reaction Methods 0.000 claims description 5
- 235000013373 food additive Nutrition 0.000 claims description 5
- 239000002778 food additive Substances 0.000 claims description 5
- 230000007062 hydrolysis Effects 0.000 claims description 5
- 238000006460 hydrolysis reaction Methods 0.000 claims description 5
- 229940038580 oat bran Drugs 0.000 claims description 5
- 229910000019 calcium carbonate Inorganic materials 0.000 claims description 3
- 230000000593 degrading effect Effects 0.000 claims description 3
- 230000007925 protein solubilization Effects 0.000 claims description 3
- 238000001799 protein solubilization Methods 0.000 claims description 3
- 239000011780 sodium chloride Substances 0.000 claims description 3
- 235000002639 sodium chloride Nutrition 0.000 claims description 3
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 claims description 3
- 229910000391 tricalcium phosphate Inorganic materials 0.000 claims description 3
- 229940078499 tricalcium phosphate Drugs 0.000 claims description 3
- 235000019731 tricalcium phosphate Nutrition 0.000 claims description 3
- 235000015112 vegetable and seed oil Nutrition 0.000 claims description 3
- 239000008158 vegetable oil Substances 0.000 claims description 3
- 239000011782 vitamin Substances 0.000 claims description 3
- 229940088594 vitamin Drugs 0.000 claims description 3
- 229930003231 vitamin Natural products 0.000 claims description 3
- 235000013343 vitamin Nutrition 0.000 claims description 3
- 235000019739 Dicalciumphosphate Nutrition 0.000 claims 2
- 229960003563 calcium carbonate Drugs 0.000 claims 2
- 235000010216 calcium carbonate Nutrition 0.000 claims 2
- NEFBYIFKOOEVPA-UHFFFAOYSA-K dicalcium phosphate Chemical compound [Ca+2].[Ca+2].[O-]P([O-])([O-])=O NEFBYIFKOOEVPA-UHFFFAOYSA-K 0.000 claims 2
- 229910000390 dicalcium phosphate Inorganic materials 0.000 claims 2
- 229940038472 dicalcium phosphate Drugs 0.000 claims 2
- 229960002668 sodium chloride Drugs 0.000 claims 2
- 150000003722 vitamin derivatives Chemical class 0.000 claims 2
- 239000012736 aqueous medium Substances 0.000 claims 1
- 239000003125 aqueous solvent Substances 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 31
- 239000000047 product Substances 0.000 description 26
- 230000006240 deamidation Effects 0.000 description 21
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 18
- 102000004190 Enzymes Human genes 0.000 description 14
- 108090000790 Enzymes Proteins 0.000 description 14
- 229940088598 enzyme Drugs 0.000 description 14
- 238000010438 heat treatment Methods 0.000 description 12
- 230000000694 effects Effects 0.000 description 11
- 239000002994 raw material Substances 0.000 description 10
- 229910021529 ammonia Inorganic materials 0.000 description 9
- 230000002255 enzymatic effect Effects 0.000 description 8
- 229920002498 Beta-glucan Polymers 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- 239000000203 mixture Substances 0.000 description 6
- 102000004882 Lipase Human genes 0.000 description 5
- 108090001060 Lipase Proteins 0.000 description 5
- 239000004367 Lipase Substances 0.000 description 5
- 102000035195 Peptidases Human genes 0.000 description 5
- 108090000637 alpha-Amylases Proteins 0.000 description 5
- 235000019421 lipase Nutrition 0.000 description 5
- 235000020262 oat milk Nutrition 0.000 description 5
- 235000019833 protease Nutrition 0.000 description 5
- 101710130006 Beta-glucanase Proteins 0.000 description 4
- 102000003820 Lipoxygenases Human genes 0.000 description 4
- 108090000128 Lipoxygenases Proteins 0.000 description 4
- 229940025131 amylases Drugs 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 238000004925 denaturation Methods 0.000 description 4
- 230000036425 denaturation Effects 0.000 description 4
- 235000019419 proteases Nutrition 0.000 description 4
- 238000003756 stirring Methods 0.000 description 4
- 102000004139 alpha-Amylases Human genes 0.000 description 3
- 229940024171 alpha-amylase Drugs 0.000 description 3
- 230000006872 improvement Effects 0.000 description 3
- 230000002779 inactivation Effects 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 238000011020 pilot scale process Methods 0.000 description 3
- 239000013049 sediment Substances 0.000 description 3
- 239000002002 slurry Substances 0.000 description 3
- FYGDTMLNYKFZSV-URKRLVJHSA-N (2s,3r,4s,5s,6r)-2-[(2r,4r,5r,6s)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2r,4r,5r,6s)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1[C@@H](CO)O[C@@H](OC2[C@H](O[C@H](O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-URKRLVJHSA-N 0.000 description 2
- BTJIUGUIPKRLHP-UHFFFAOYSA-N 4-nitrophenol Chemical compound OC1=CC=C([N+]([O-])=O)C=C1 BTJIUGUIPKRLHP-UHFFFAOYSA-N 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 235000019484 Rapeseed oil Nutrition 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000007515 enzymatic degradation Effects 0.000 description 2
- 239000000835 fiber Substances 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 210000004080 milk Anatomy 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 238000004062 sedimentation Methods 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000010025 steaming Methods 0.000 description 2
- 235000007558 Avena sp Nutrition 0.000 description 1
- 102000006395 Globulins Human genes 0.000 description 1
- 108010044091 Globulins Proteins 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 102000014171 Milk Proteins Human genes 0.000 description 1
- 108010011756 Milk Proteins Proteins 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 1
- 235000019647 acidic taste Nutrition 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 235000020167 acidified milk Nutrition 0.000 description 1
- 230000002009 allergenic effect Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 235000019658 bitter taste Nutrition 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000013065 commercial product Substances 0.000 description 1
- 235000020247 cow milk Nutrition 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 238000010908 decantation Methods 0.000 description 1
- 230000003297 denaturating effect Effects 0.000 description 1
- 230000001804 emulsifying effect Effects 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000005187 foaming Methods 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 238000000227 grinding Methods 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 235000004213 low-fat Nutrition 0.000 description 1
- 235000021239 milk protein Nutrition 0.000 description 1
- 235000013384 milk substitute Nutrition 0.000 description 1
- 235000020124 milk-based beverage Nutrition 0.000 description 1
- 238000003801 milling Methods 0.000 description 1
- 125000000636 p-nitrophenyl group Chemical group [H]C1=C([H])C(=C([H])C([H])=C1*)[N+]([O-])=O 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 235000020245 plant milk Nutrition 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000005096 rolling process Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000001117 sulphuric acid Substances 0.000 description 1
- 235000011149 sulphuric acid Nutrition 0.000 description 1
- 235000011875 whole grain product Nutrition 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L7/00—Cereal-derived products; Malt products; Preparation or treatment thereof
- A23L7/10—Cereal-derived products
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
- A23L2/52—Adding ingredients
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C11/00—Milk substitutes, e.g. coffee whitener compositions
- A23C11/02—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins
- A23C11/10—Milk substitutes, e.g. coffee whitener compositions containing at least one non-milk component as source of fats or proteins containing or not lactose but no other milk components as source of fats, carbohydrates or proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
- A23L2/38—Other non-alcoholic beverages
- A23L2/382—Other non-alcoholic beverages fermented
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Their preparation
- A23L2/52—Adding ingredients
- A23L2/68—Acidifying substances
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- 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 COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/30—Dietetic or nutritional methods, e.g. for losing weight
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L7/00—Cereal-derived products; Malt products; Preparation or treatment thereof
- A23L7/10—Cereal-derived products
- A23L7/104—Fermentation of farinaceous cereal or cereal material; Addition of enzymes or microorganisms
- A23L7/107—Addition or treatment with enzymes not combined with fermentation with microorganisms
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2250/00—Food ingredients
- A23V2250/54—Proteins
- A23V2250/548—Vegetable protein
- A23V2250/5484—Oat protein
Definitions
- the present invention relates to a liquid oat base, in particular a liquid oat base for use as a milk substitute or a food additive, and to a method for its manufacture.
- Oat drinks (“oat milk”) for use as cow milk substitutes (EP 731646 B1; EP 1124441 B1; U.S. Pat. No. 6,451,369 B1) and as a raw material for other non-dairy milk products (U.S. Pat. No. 7,160,564 B2) are known in the art. They are preferred by many customers for various reasons, such as for their content of soluble ⁇ -glucan fiber beneficial to health, their lack of potentially allergenic proteins and of lactose, which cannot be digested by the majority of the global population.
- the soluble protein content of oat milk is about 0.5 to about 1.0% by weight.
- the starting material such as oat flour or oat bran or the whole oats from which it is made or an aqueous suspending or mixture of it is heated to a temperature and for a time sufficient to substantially prevent the development of endogenous enzymatic activity, in particular lipase/lipoxygenase activity, but also ⁇ -glucanase activity, during the respective process.
- Known oat drinks may be termed “oat bases” since, in addition to be used as drinks, in particular milk drinks, they can be used as a base for food other products, such as oat yogurt or oat batter, or be used as a food additive.
- oat milk typically 0.5% by weight
- fat in form of vegetable oil such as rapeseed oil
- EP 976 829 A1 discloses a protein deamidating enzyme and a process for its production.
- EP 1 371 734 A1 discloses a method of denaturating milk protein by a deamidating enzyme to improve its sensitivity to protease and its emulsifying, foaming and gelling characteristics.
- EP 1 839 491 discloses a dairy product and a method of its production by contacting milk with a deamidating enzyme to suppress acidic and bitter taste.
- WO 2008/138900 A2 discloses a method for producing an acidified milk drink by contacting raw or processed milk with a deamidating enzyme.
- Another object of the invention is to provide said improvements while maintaining or even improving the organoleptic properties of the drink.
- a further object of the invention is to provide a process for producing the improved oat drink or base.
- an oat base of the aforementioned kind having an improved content of soluble oat protein.
- “Improved protein content” is a higher protein content than obtainable by methods known in the art from a given oat raw material with the proviso that the improved content is not due to the use of protease (peptidase/proteinase).
- the oat base of the invention is provided by degrading an oats material with one or more amylases and protein-deamidase.
- the protein-deamidase is one capable of deamidating high-molecular oat protein, such as oat globulin.
- the protein-deamidase does not comprise substantial protease (peptidase) activity.
- the protein-deamidase of the invention is preferably free from protease activity. Examples for protein-deamidases useful in the invention are disclosed in EP 976829 B1. A preferred amount of protein-deamidase is from 0.5-20 U/g oat protein.
- deamidation is carried out in parallel amidolysis, that is, with starch degradation by amylase(s). “In parallel with amidolysis” is understood as simultaneous with the enzymatic degradation of starch by amylase(s). In the process of the invention deamidation of oat protein may however be continued even after amidolysis has ceased or substantially ceased.
- the process of the invention can be stopped at a desired viscosity, such as at a viscosity of from 100 cP to 200 cP or from 50 cP to 100 cP or from 25 cP to 50 cP or from 10 cP to 25 cP (sp2/60 rpm/25 ⁇ 2° C.).
- the process of the invention is preferably stopped by heating to a temperature at which any enzymatic activity is destroyed within a short time, such as within ten seconds or one minute or five minutes, said temperature being >80° C., preferably greater than 90° C., in particular greater than 100° C., such as about 105° C., at which temperature heating for about 10 seconds is sufficient to destroy any enzymatic activity.
- the improved oat base of the invention differs from prior art oat bases (oat drinks) by its increased content of soluble oat protein.
- soluble signifies “water soluble”.
- the improvement in soluble protein content obtainable by the method of the invention is 10 percent by weight and up to 20 percent by weight or more.
- the content of soluble protein in the oat base is not one increased by addition of soluble protein to the base or to the raw material from which it is made or during the process by which it is manufactured but by use of an appropriate oat raw material and an appropriate protein solubilization process. It is preferable to use a raw material with a high content of protein preserved in its natural state. “Preserved in its (a) natural state” signifies that the protein in the raw material has not been denaturated or has only been denaturated to a minor extent, such as by 10% by weight or 20% by weight.
- Oats used for producing oat drinks is dry- or wet-heated prior to use as starting material for producing oat bases or drinks.
- the purpose with the heat treatment is twofold. On the one hand, the purpose is to destroy beta-glucanase present and/or to prevent it from being formed during starch hydrolysis so as to preserve water-soluble beta-glucans in their native state.
- Beta-glucans in their native state are high-molecular beta-glucans, such as of a molecular weight of 50,000 D or more. High molecular beta-glucans are considered to constitute a valuable health-promoting component of oat drinks. Inactivation of beta-glucanase by heat treatment is however only indicated if the oat drink to be manufactures is desired to contain substantial amounts of beta-glucans.
- the purpose with the traditional heat treatment is to inactivate lipase and lipoxygenase.
- Inactivation of lipase and lipoxygenase is indicated to prevent the product from turning rancid.
- the need of inactivating lipase and lipoxigenase can be avoided by removing the lipids of the raw material, such as by extraction with ethanol or supercritical carbon dioxide. Preferably at least 90% and even at least 95% of the lipids are removed.
- water-soluble protein in untreated oats is about 60% to about 70% weight of total protein, it is only about 30% weight in microwave-treated oats (Sk ⁇ nemöllan, Sweden) and in steam-treated (102° C. for 50 min, then air-dried (110° C.-120° C. min for 50 min) oats.
- this kind of heat treatment in particular steaming, should be avoided or at least be kept as short as possible and/or carried out at a temperature as low as possible to keep oat protein denaturation low. If avoided, the lipids should be removed from the oats. If heating is the preferred method of preventing the product from turning rancid and from preventing substantial degradation of ⁇ -glucan, a compromise between heating temperature and/or length of heating, at the one hand, and completeness of inactivation of ⁇ -glucanase and lipase/lipoxygenase, at the other hand is attempted.
- a preferred raw material for use in the invention is dehulled or hulless/naked, dry milled oat flour that has not been heat treated, in particular steamed.
- dry milled oat flour that has not been heat treated or dry milled flour of any oats fraction can also be used.
- Particularly preferred is the use of dry milled non-heat treated oats, non-heat treated oat bran, and non-steamed oats.
- heating of oats in any form at a temperature of up to about 50° C. or even up to about 65° C. for a few hours, such as for one or two or even five hours, does not result in substantial denaturation.
- heating such oats material for a corresponding time period at a temperature of 80° C. or more does result in a substantial reduction of soluble protein, in particular if the material is in a humid state.
- Steaming of oats in any form results in substantial denaturation, such as denaturation of 30% or more and even of 50% of more. Consequently, steamed oats materials, such as, for instance, those disclosed in U.S. Pat. No. 6,165,365 A and U.S. Pat. No. 7,494,683 B2, are not preferred for use in the present invention.
- the oat base of the invention is prepared by milling groats (dehulled oats) with water to obtain a mash containing from 8% by weight to 13% by weight dry substance, then adding amylase(s) and degrading the oat starch at a temperature of from 50° C. to 75° C.
- the amylase may be beta- and alpha amylase or a mixture thereof, the amylases being added as a mixture or their mixture in the mash being formed by their simultaneous or sequential addition.
- amylases are added in amount(s) sufficient for significant hydrolysis of starch over a time period of from 0.5 h to 4 hrs, in particular from about 1 h to about 2 hrs, hydrolysis of more than 50% by weight of the starch, in particular of more than 80% by weight or even more than 90% weight being considered significant.
- amylase(s) are added in an amount to provide amylase activity of from 140 to 250 Betamyl-3 units and from 0.5 to 4 Ceralpha units per g of starch, in particular of about 180 Betamyl-3 units and about 1 Ceralpha unit per g of starch.
- liquid oat base prepared by the process of the invention and a liquid oat base comprising oat protein deamidated by protein deamidase. It is preferred for the oat base protein to comprise 10% by weight or 20% by weight or more of protein deamidated by protein deamidase.
- liquid oat base of the invention as a food, a food additive or a starting material for production of a food, all intended for human consumption.
- composition Prepared from steam treated Swedish oat grain by grinding in a rolling mill.
- Composition (% by weight): Protein 18, fat 7, carbohydrate 45, fiber 16%, water 9.5.
- Protein-glutaminase “Amano 50”, 50 U/g (Amano Inc., Japan). Commercial alpha-amylase and beta-amylase are available from various commercial sources.
- One Ceralpha unit is defined as the amount of enzyme required to release one micromole of p-nitrophenol from BPNPG7 (non-reducing end blocked p-nitrophenyl maltoheptaoside) in one minute under defined assay conditions: https://secure.megazyme.com/files/BOOKLET/K-BETA3_1010_DATA.pdf
- BNP ⁇ -G3 p-nitrophenyl- ⁇ -D-maltotrioside unit is defined as the amount of enzyme required to release one micromole of p-nitrophenol from PNP ⁇ -G3 in one minute under defined assay conditions: https://secure.megazyme.com/files/BOOKLET/K-BETA3_1010_DATA.pdf
- One activity unit (U) is defined as the quantity of enzyme producing one ⁇ mol of ammonia per min in the reaction with 10 mM aqueous benzylocarbonyl-L-glutaminylglycine (Cbz-Gln-Gly).
- Dehulled, steam treated oat kernels (675 kg) were wet ground in a colloidal mill at a temperature of 54° C. and directly fed into a stainless steel enzyme treatment tank over a period of about 20 min. Stirring was started at a mash volume of about 100 L. About 7.5 L of an aqueous solution of alpha- and beta-amylase (1 Ceralpha unit per 180 Betamyl-3 units per g of starch) was used. Enzyme activity may vary depending on the commercial source of the enzymes; in this experiment the total weight of amylases was 432 g. The enzyme solution was fed into the tank in parallel with the mash over a period of about 12 min at the end of which about 3000 L of the mash had been fed into the tank. The rest of the mash was fed into the tank over a period of about 8 min to bring the total contents of the tank to about 5600 L. The temperature of the mash was kept constant at 56° C.
- PG (687.5 g) was dissolved in 1.5 L water at room temperature.
- the PG solution was added to the mash at a viscosity of 160.5 (sp2/60 rpm/25 ⁇ 2° C.).
- Stirring was continued for about 120 min at a temperature of about 56° C. to reach a mash viscosity of 35 (sp2/60 rpm/25 ⁇ 2° C.) and a pH of 6.6. Any enzyme activity was then destroyed by heating the product to 95° C.
- the mash was cooled to room temperature and decanted. Decantation can be omitted if a whole grain product is to be produced.
- the thus produced oat base of the invention can be transferred into a formulation tank in which rapeseed oil, vitamins, sodium chloride, di- and tricalcium phosphate, and calcium carbonate is added.
- the thus obtained enriched oat drink has a viscosity (sp2/60 rpm/25 ⁇ 2° C.) of 17.5 cP and a pH of 6.8.
- the formulated oat drink or oat milk is transferred to a storage tank from which it is dispensed for UHT treatment and packaging.
- dehulled steam treated oat kernels instead of dehulled steam treated oat kernels also corresponding naked kernels may be used, for instance, as a starting material.
- Example 2 Modified and Down-Scaled (1:10 5 ) Process of Example 1
- Example 3 Modified and Down-Scaled Process of Example 1
- Example 4 Modified and Down-Scaled Process of Example 1
- the oat base or drink used in the example was prepared according to the method disclosed in European patent no. 731 646.
- This oat drink is a commercial product manufactured by Oatly A B, Landskrona, Sweden.
- Table 1 important features of a number of products according to the invention are shown. Also shown are corresponding features of deamidation products obtained from dry-milled heat-treated oats. The products were obtained in absence of deamidase (0 U) and in presence of deamidase at two deamidase addition regimes (1 U; 2 ⁇ 0.5 U/g oat protein). From Table 1 it is evident that the content of total protein is substantially increased in the presence of deamidase. It is also evident that, at otherwise identical conditions, a non-heat treated starting material yields a product with higher protein content than a corresponding heat-treated starting material.
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Abstract
Description
- The present invention relates to a liquid oat base, in particular a liquid oat base for use as a milk substitute or a food additive, and to a method for its manufacture.
- Oat drinks (“oat milk”) for use as cow milk substitutes (EP 731646 B1; EP 1124441 B1; U.S. Pat. No. 6,451,369 B1) and as a raw material for other non-dairy milk products (U.S. Pat. No. 7,160,564 B2) are known in the art. They are preferred by many customers for various reasons, such as for their content of soluble β-glucan fiber beneficial to health, their lack of potentially allergenic proteins and of lactose, which cannot be digested by the majority of the global population. The soluble protein content of oat milk is about 0.5 to about 1.0% by weight. In the prior art processes for preparing oat milk the starting material, such as oat flour or oat bran or the whole oats from which it is made or an aqueous suspending or mixture of it is heated to a temperature and for a time sufficient to substantially prevent the development of endogenous enzymatic activity, in particular lipase/lipoxygenase activity, but also β-glucanase activity, during the respective process. Known oat drinks may be termed “oat bases” since, in addition to be used as drinks, in particular milk drinks, they can be used as a base for food other products, such as oat yogurt or oat batter, or be used as a food additive.
- Due to the low fat content of oat milk (typically 0.5% by weight) fat in form of vegetable oil, such as rapeseed oil, is often added to the product.
- In spite of the commercial success of oat drinks available on the market there is room for further improvement, in particular in respect of increasing the protein content of the drinks. Processes for producing oat drinks known in the art do not adequately access the protein in oat raw material.
- It is known to increase the content of water soluble protein in oat drinks by the use of proteinase in addition to amylase(s) in the enzymatic degradation of oat raw material. The use of proteinase however results in the formation of low-molecular peptides, which may change the organoleptic properties of the drinks.
- EP 976 829 A1 discloses a protein deamidating enzyme and a process for its production. EP 1 371 734 A1 discloses a method of denaturating milk protein by a deamidating enzyme to improve its sensitivity to protease and its emulsifying, foaming and gelling characteristics. EP 1 839 491 discloses a dairy product and a method of its production by contacting milk with a deamidating enzyme to suppress acidic and bitter taste. WO 2008/138900 A2 discloses a method for producing an acidified milk drink by contacting raw or processed milk with a deamidating enzyme.
- In addition to/separate from deamidation by a deamidating enzyme glutamyl and asparagyl residues in peptides and proteins have been observed to undergo non-enzymatic deamidation in vitro and in vivo (Robinson N A, Protein Deamidation. Proc Nat Acad Sci, 99 (2002)5283-5288—https://www.pnas.org/content/99/8/5283.full and literature cited therein).
- It is an object of the invention to provide an oat drink or base of the aforementioned kind, which has improved protein content.
- Another object of the invention is to provide said improvements while maintaining or even improving the organoleptic properties of the drink.
- A further object of the invention is to provide a process for producing the improved oat drink or base.
- Additional objects of the invention will become evident from the following summary of the invention, a number of examples describing preferred embodiments thereof, and the appended claims.
- According to the present invention is provided an oat base of the aforementioned kind having an improved content of soluble oat protein. “Improved protein content” is a higher protein content than obtainable by methods known in the art from a given oat raw material with the proviso that the improved content is not due to the use of protease (peptidase/proteinase).
- The oat base of the invention is provided by degrading an oats material with one or more amylases and protein-deamidase.
- According to one preferred aspect of the invention the protein-deamidase is one capable of deamidating high-molecular oat protein, such as oat globulin.
- According to a preferred aspect of the invention the protein-deamidase does not comprise substantial protease (peptidase) activity. The protein-deamidase of the invention is preferably free from protease activity. Examples for protein-deamidases useful in the invention are disclosed in EP 976829 B1. A preferred amount of protein-deamidase is from 0.5-20 U/g oat protein.
- According to another preferred aspect of the invention, deamidation is carried out in parallel amidolysis, that is, with starch degradation by amylase(s). “In parallel with amidolysis” is understood as simultaneous with the enzymatic degradation of starch by amylase(s). In the process of the invention deamidation of oat protein may however be continued even after amidolysis has ceased or substantially ceased.
- The process of the invention can be stopped at a desired viscosity, such as at a viscosity of from 100 cP to 200 cP or from 50 cP to 100 cP or from 25 cP to 50 cP or from 10 cP to 25 cP (sp2/60 rpm/25±2° C.). The process of the invention is preferably stopped by heating to a temperature at which any enzymatic activity is destroyed within a short time, such as within ten seconds or one minute or five minutes, said temperature being >80° C., preferably greater than 90° C., in particular greater than 100° C., such as about 105° C., at which temperature heating for about 10 seconds is sufficient to destroy any enzymatic activity.
- The improved oat base of the invention differs from prior art oat bases (oat drinks) by its increased content of soluble oat protein. In this application “soluble” signifies “water soluble”. The improvement in soluble protein content obtainable by the method of the invention is 10 percent by weight and up to 20 percent by weight or more.
- Thus, according to the present invention, the content of soluble protein in the oat base is not one increased by addition of soluble protein to the base or to the raw material from which it is made or during the process by which it is manufactured but by use of an appropriate oat raw material and an appropriate protein solubilization process. It is preferable to use a raw material with a high content of protein preserved in its natural state. “Preserved in its (a) natural state” signifies that the protein in the raw material has not been denaturated or has only been denaturated to a minor extent, such as by 10% by weight or 20% by weight.
- Oats used for producing oat drinks is dry- or wet-heated prior to use as starting material for producing oat bases or drinks. The purpose with the heat treatment is twofold. On the one hand, the purpose is to destroy beta-glucanase present and/or to prevent it from being formed during starch hydrolysis so as to preserve water-soluble beta-glucans in their native state. Beta-glucans in their native state are high-molecular beta-glucans, such as of a molecular weight of 50,000 D or more. High molecular beta-glucans are considered to constitute a valuable health-promoting component of oat drinks. Inactivation of beta-glucanase by heat treatment is however only indicated if the oat drink to be manufactures is desired to contain substantial amounts of beta-glucans.
- On the other hand and, in a more general manner, the purpose with the traditional heat treatment is to inactivate lipase and lipoxygenase. Inactivation of lipase and lipoxygenase is indicated to prevent the product from turning rancid. According to a preferred aspect of the invention the need of inactivating lipase and lipoxigenase can be avoided by removing the lipids of the raw material, such as by extraction with ethanol or supercritical carbon dioxide. Preferably at least 90% and even at least 95% of the lipids are removed.
- While the content of water-soluble protein in untreated oats is about 60% to about 70% weight of total protein, it is only about 30% weight in microwave-treated oats (Skånemöllan, Sweden) and in steam-treated (102° C. for 50 min, then air-dried (110° C.-120° C. min for 50 min) oats.
- In the method of the invention this kind of heat treatment, in particular steaming, should be avoided or at least be kept as short as possible and/or carried out at a temperature as low as possible to keep oat protein denaturation low. If avoided, the lipids should be removed from the oats. If heating is the preferred method of preventing the product from turning rancid and from preventing substantial degradation of β-glucan, a compromise between heating temperature and/or length of heating, at the one hand, and completeness of inactivation of β-glucanase and lipase/lipoxygenase, at the other hand is attempted.
- A preferred raw material for use in the invention is dehulled or hulless/naked, dry milled oat flour that has not been heat treated, in particular steamed. However, wet milled oat flour that has not been heat treated or dry milled flour of any oats fraction can also be used. Particularly preferred is the use of dry milled non-heat treated oats, non-heat treated oat bran, and non-steamed oats.
- According to the invention it has been found that heating of oats in any form at a temperature of up to about 50° C. or even up to about 65° C. for a few hours, such as for one or two or even five hours, does not result in substantial denaturation. On the other hand, heating such oats material for a corresponding time period at a temperature of 80° C. or more does result in a substantial reduction of soluble protein, in particular if the material is in a humid state. Steaming of oats in any form results in substantial denaturation, such as denaturation of 30% or more and even of 50% of more. Consequently, steamed oats materials, such as, for instance, those disclosed in U.S. Pat. No. 6,165,365 A and U.S. Pat. No. 7,494,683 B2, are not preferred for use in the present invention.
- According to one preferred aspect of the invention the oat base of the invention is prepared by milling groats (dehulled oats) with water to obtain a mash containing from 8% by weight to 13% by weight dry substance, then adding amylase(s) and degrading the oat starch at a temperature of from 50° C. to 75° C. The amylase may be beta- and alpha amylase or a mixture thereof, the amylases being added as a mixture or their mixture in the mash being formed by their simultaneous or sequential addition.
- The amylases are added in amount(s) sufficient for significant hydrolysis of starch over a time period of from 0.5 h to 4 hrs, in particular from about 1 h to about 2 hrs, hydrolysis of more than 50% by weight of the starch, in particular of more than 80% by weight or even more than 90% weight being considered significant.
- Typically the amylase(s) are added in an amount to provide amylase activity of from 140 to 250 Betamyl-3 units and from 0.5 to 4 Ceralpha units per g of starch, in particular of about 180 Betamyl-3 units and about 1 Ceralpha unit per g of starch.
- Also disclosed according to the invention is a liquid oat base prepared by the process of the invention and a liquid oat base comprising oat protein deamidated by protein deamidase. It is preferred for the oat base protein to comprise 10% by weight or 20% by weight or more of protein deamidated by protein deamidase.
- According to the invention is furthermore disclosed the use of the liquid oat base of the invention as a food, a food additive or a starting material for production of a food, all intended for human consumption.
- Oat Kernels:
- Dehulled, steam treated, wet ground or dry ground.
- Oat Bran (Frebaco Kvarn A B, Lidköping, Sweden):
- Prepared from steam treated Swedish oat grain by grinding in a rolling mill. Composition (% by weight): Protein 18, fat 7, carbohydrate 45, fiber 16%, water 9.5.
- Enzymes:
- Protein-glutaminase “Amano 50”, 50 U/g (Amano Inc., Japan). Commercial alpha-amylase and beta-amylase are available from various commercial sources.
- Alpha-Amylase Activity:
- One Ceralpha unit is defined as the amount of enzyme required to release one micromole of p-nitrophenol from BPNPG7 (non-reducing end blocked p-nitrophenyl maltoheptaoside) in one minute under defined assay conditions: https://secure.megazyme.com/files/BOOKLET/K-BETA3_1010_DATA.pdf
- Beta-Amylase Activity:
- One BNPβ-G3 (p-nitrophenyl-β-D-maltotrioside) unit is defined as the amount of enzyme required to release one micromole of p-nitrophenol from PNPβ-G3 in one minute under defined assay conditions: https://secure.megazyme.com/files/BOOKLET/K-BETA3_1010_DATA.pdf
- Protein-Glutaminase Activity:
- One activity unit (U) is defined as the quantity of enzyme producing one μmol of ammonia per min in the reaction with 10 mM aqueous benzylocarbonyl-L-glutaminylglycine (Cbz-Gln-Gly).
- Viscosity:
- Measured with a Brookfield Visco DV-II+ instrument (https://www.brookfieldengineering.com/products/viscosimeters/laboratory-dv-ii.asp.
- Dehulled, steam treated oat kernels (675 kg) were wet ground in a colloidal mill at a temperature of 54° C. and directly fed into a stainless steel enzyme treatment tank over a period of about 20 min. Stirring was started at a mash volume of about 100 L. About 7.5 L of an aqueous solution of alpha- and beta-amylase (1 Ceralpha unit per 180 Betamyl-3 units per g of starch) was used. Enzyme activity may vary depending on the commercial source of the enzymes; in this experiment the total weight of amylases was 432 g. The enzyme solution was fed into the tank in parallel with the mash over a period of about 12 min at the end of which about 3000 L of the mash had been fed into the tank. The rest of the mash was fed into the tank over a period of about 8 min to bring the total contents of the tank to about 5600 L. The temperature of the mash was kept constant at 56° C.
- Protein-Glutaminase (PG) Dosing.
- PG (687.5 g) was dissolved in 1.5 L water at room temperature. The PG solution was added to the mash at a viscosity of 160.5 (sp2/60 rpm/25±2° C.). Stirring was continued for about 120 min at a temperature of about 56° C. to reach a mash viscosity of 35 (sp2/60 rpm/25±2° C.) and a pH of 6.6. Any enzyme activity was then destroyed by heating the product to 95° C. The mash was cooled to room temperature and decanted. Decantation can be omitted if a whole grain product is to be produced.
- The thus produced oat base of the invention can be transferred into a formulation tank in which rapeseed oil, vitamins, sodium chloride, di- and tricalcium phosphate, and calcium carbonate is added. The thus obtained enriched oat drink has a viscosity (sp2/60 rpm/25±2° C.) of 17.5 cP and a pH of 6.8. The formulated oat drink or oat milk is transferred to a storage tank from which it is dispensed for UHT treatment and packaging.
- Product Analysis.
- Deamidation of product: 7.3% of total releaseable ammonia (by treatment with 2 N sulphuric acid at 100° C. for 4 h). Deamidation of control (non-enzymatic deamidation): 1.6% of total releaseable ammonia (same process in absence of PG). Soluble protein: 78% of total protein (product of the invention) v. 64% of total protein (control).
- Instead of dehulled steam treated oat kernels also corresponding naked kernels may be used, for instance, as a starting material.
- Wet-milled oat slurry is heated to 60° C. under stirring. Alpha- and beta-amylase as well as protein glutaminase (1 U/g of oat protein) are added and reacted with the slurry under stirring at 60° C. for two hours. The slurry is the heated to 95° C. for 5 min. Insoluble matter is removed by pulse centrifugation (pulses of 1100 g) and analyzed.
- Product Analysis.
- Deamidation of product: 6.9% of total releaseable ammonia. Deamidation of control (non-enzymatic deamidation): 1.9% of total releaseable ammonia (same process in absence of PG). Soluble protein: 84% of total protein (product of the invention) v. 56% of total protein (control).
- As Example 2 but with heat treated dry milled and sieved oat kernels, fraction size <0.5 mm mixed with water to a dry weight of 11%.
- Product Analysis.
- Deamidation of product: 6.1% of total releaseable ammonia. Deamidation of control (non-enzymatic deamidation): 1.5% of total releaseable ammonia (same process in absence of PG). Soluble protein: 59% of total protein (product of the invention) v. 48% of total protein (control).
- As Example 2 but with non-heat treated dry milled and sieved oat kernels, fraction size <0.5 mm mixed with water to a dry weight of 11%.
- Product Analysis.
- Deamidation of product: 8.9% of total releaseable ammonia. Deamidation of control (non-enzymatic deamidation): 1.5% of total releaseable ammonia (same process in absence of PG). Soluble protein: 81% of total protein (product of the invention) v. 62% of total protein (control).
- The oat base or drink used in the example was prepared according to the method disclosed in European patent no. 731 646. This oat drink is a commercial product manufactured by Oatly A B, Landskrona, Sweden. In Table 1 important features of a number of products according to the invention are shown. Also shown are corresponding features of deamidation products obtained from dry-milled heat-treated oats. The products were obtained in absence of deamidase (0 U) and in presence of deamidase at two deamidase addition regimes (1 U; 2×0.5 U/g oat protein). From Table 1 it is evident that the content of total protein is substantially increased in the presence of deamidase. It is also evident that, at otherwise identical conditions, a non-heat treated starting material yields a product with higher protein content than a corresponding heat-treated starting material.
- It is furthermore evident that that, at otherwise identical conditions, sequential addition of deamidase (2×0.5 U) yields a product of higher protein content than obtained by a single addition of the same amount of amylase (1 U). A higher protein content of the product is paralleled by increased emulsion stability (reduced sedimentation rate) of the product.
-
TABLE 1 Deamidation of oat drink at laboratory and pilot plant scale Protein- Glutaminase, Soluble protein, Total Droplet Oat raw U/g of Deamidation g/100 g (% of protein size (μm), material Oat Protein (%) total) g/100 g 1.5% fat Sedimentation Laboratory scale Wet-milled 0 U 19 0.71 (57%) 0.84 3.2 14% UPH** 1 U 6.7 0.90 (72%) 0.92 1.7 2 white PH* 2 × 0.5 U*** 6.9 1.06 (87%) 0.95 0.8 2 white PH Dry-milled, 0 U 1.5 0.59 (46%) 0.64 4.5 17% UPH heat treated 1 U 6.1 0.75 (59%) 0.81 3.6 No sediment 2 × 0.5 U*** 8.6 0.80 (63%) 0.80 4.0 No sediment Dry milled, 0 U 1.5 0.88 (64%) 0.80 2.6 38% UPH non-heat 1 U 8.9 1.16 (81%) 0.92 1.2 30% UPH treated 2 × 0.5 U*** 9.5 1.26 (93%) 0.94 1.2 28% UPH Oat bran 0 U 1.8 0.41 (17%) 1.25 7.1 13% UPH 1 U 5.9 1.05 (42%) 1.62 6.3 7% UPH 2 × 0.5 U*** 6.1 1.09 (44%) 1.60 5.6 4% UPH Small pilot scale Wet-milled 0 U 2.3 0.65 (56%) 0.82 15.8 10% UPH 1 U 7.9 0.70 (67%) 0.80 15.8 2 white PH 2 × 0.5 U*** 13.0 0.83 (72%) 1.01 17.8 No sediment Large pilot scale Wet-milled 0 U 1.6 0.70 (64%) 0.75 7.9 63% UPH 2 × 0.5 U*** 7.3 1.00 (78%) 0.91 10.0 2 white PH *PH = Phase; **UPH = Upper phase; ***0.5 U added to each of two amylase enzymation steps
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WO2020150583A1 (en) * | 2019-01-18 | 2020-07-23 | Ripple Foods, Pbc | Non-dairy analogs and beverages with deamidated plant proteins and processes for making such products |
WO2023126061A1 (en) * | 2021-12-30 | 2023-07-06 | Oatly Ab | Liquid oat composition and method for production thereof |
US11771121B1 (en) | 2021-01-05 | 2023-10-03 | Chobani Llc | Plant-based zero sugar food product and associated method |
EP4238422A4 (en) * | 2020-10-30 | 2024-10-09 | Amano Enzyme Inc | Method for manufacturing processed article of vegetable protein food/beverage product in which aroma is enhanced |
EP4238421A4 (en) * | 2020-10-30 | 2024-10-16 | Amano Enzyme Inc | Method for producing vegetable protein-processed product having improved food texture |
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US9510614B2 (en) | 2008-11-04 | 2016-12-06 | The Quaker Oats Company | Food products prepared with soluble whole grain oat flour |
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JP6511400B2 (en) | 2019-05-15 |
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JP2018075029A (en) | 2018-05-17 |
US20150351432A1 (en) | 2015-12-10 |
CN105007757A (en) | 2015-10-28 |
CA2899717C (en) | 2017-05-30 |
EP2953482B1 (en) | 2019-01-16 |
PT2953482T (en) | 2019-05-13 |
WO2014123466A1 (en) | 2014-08-14 |
EP2953482A4 (en) | 2016-11-09 |
RU2015125371A (en) | 2017-03-13 |
US20220015399A1 (en) | 2022-01-20 |
DK2953482T3 (en) | 2019-04-23 |
PL2953482T3 (en) | 2019-07-31 |
RU2616802C2 (en) | 2017-04-18 |
ES2719698T3 (en) | 2019-07-12 |
MY181577A (en) | 2020-12-29 |
AU2014215729B2 (en) | 2015-11-26 |
HK1212562A1 (en) | 2016-06-17 |
KR101773155B1 (en) | 2017-08-30 |
HRP20190518T1 (en) | 2019-05-03 |
KR20150113200A (en) | 2015-10-07 |
RS58501B1 (en) | 2019-04-30 |
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