IE44072B1 - Novel food compositions containing microbial proteins - Google Patents
Novel food compositions containing microbial proteinsInfo
- Publication number
- IE44072B1 IE44072B1 IE2430/76A IE243076A IE44072B1 IE 44072 B1 IE44072 B1 IE 44072B1 IE 2430/76 A IE2430/76 A IE 2430/76A IE 243076 A IE243076 A IE 243076A IE 44072 B1 IE44072 B1 IE 44072B1
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- 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
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- 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
- A23L11/00—Pulses, i.e. fruits of leguminous plants, for production of food; Products from legumes; Preparation or treatment thereof
- A23L11/60—Drinks from legumes, e.g. lupine drinks
- A23L11/65—Soy drinks
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- A—HUMAN NECESSITIES
- A21—BAKING; EDIBLE DOUGHS
- A21D—TREATMENT, e.g. PRESERVATION, OF FLOUR OR DOUGH, e.g. BY ADDITION OF MATERIALS; BAKING; BAKERY PRODUCTS; PRESERVATION THEREOF
- A21D2/00—Treatment of flour or dough by adding materials thereto before or during baking
- A21D2/08—Treatment of flour or dough by adding materials thereto before or during baking by adding organic substances
- A21D2/24—Organic nitrogen compounds
- A21D2/26—Proteins
- A21D2/267—Microbial proteins
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- 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
- A23C19/00—Cheese; Cheese preparations; Making thereof
- A23C19/06—Treating cheese curd after whey separation; Products obtained thereby
- A23C19/09—Other cheese preparations; Mixtures of cheese with other foodstuffs
- A23C19/093—Addition of non-milk fats or non-milk proteins
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- 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
- A23C20/00—Cheese substitutes
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- 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
- A23C21/00—Whey; Whey preparations
- A23C21/04—Whey; Whey preparations containing non-milk components as source of fats or proteins
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- 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
- A23C9/00—Milk preparations; Milk powder or milk powder preparations
- A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
- A23C9/13—Fermented milk preparations; Treatment using microorganisms or enzymes using additives
- A23C9/1315—Non-milk proteins or fats; Seeds, pulses, cereals or soja; Fatty acids, phospholipids, mono- or diglycerides or derivatives therefrom; Egg products
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23D—EDIBLE OILS OR FATS, e.g. MARGARINES, SHORTENINGS, COOKING OILS
- A23D9/00—Other edible oils or fats, e.g. shortenings, cooking oils
- A23D9/007—Other edible oils or fats, e.g. shortenings, cooking oils characterised by ingredients other than fatty acid triglycerides
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- 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
- A23J1/18—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from yeasts
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- 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
- A23J3/20—Proteins from microorganisms or unicellular algae
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/22—Working-up of proteins for foodstuffs by texturising
- A23J3/225—Texturised simulated foods with high protein content
- A23J3/227—Meat-like textured foods
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K50/00—Feeding-stuffs specially adapted for particular animals
- A23K50/40—Feeding-stuffs specially adapted for particular animals for carnivorous animals, e.g. cats or dogs
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- 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
- A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
- A23L13/40—Meat products; Meat meal; Preparation or treatment thereof containing additives
- A23L13/42—Additives other than enzymes or microorganisms in meat products or meat meals
- A23L13/424—Addition of non-meat animal protein material, e.g. blood, egg, dairy products, fish; Proteins from microorganisms, yeasts or fungi
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- 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
- A23L33/19—Dairy proteins
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- 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
- A23L33/195—Proteins from microorganisms
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- 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
- A23L9/00—Puddings; Cream substitutes; Preparation or treatment thereof
- A23L9/10—Puddings; Dry powder puddings
- A23L9/12—Ready-to-eat liquid or semi-liquid desserts, e.g. puddings, not to be mixed with liquids, e.g. water, milk
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- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Polymers & Plastics (AREA)
- Food Science & Technology (AREA)
- Health & Medical Sciences (AREA)
- Nutrition Science (AREA)
- Mycology (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Botany (AREA)
- Agronomy & Crop Science (AREA)
- Molecular Biology (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Biophysics (AREA)
- Animal Husbandry (AREA)
- Birds (AREA)
- Zoology (AREA)
- Cell Biology (AREA)
- Biotechnology (AREA)
- Dairy Products (AREA)
- Bakery Products And Manufacturing Methods Therefor (AREA)
- Confectionery (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- General Preparation And Processing Of Foods (AREA)
- Non-Alcoholic Beverages (AREA)
- Edible Oils And Fats (AREA)
- Grain Derivatives (AREA)
Abstract
The food composition, which may be used in a marshmallow, an imitation butter milk, a cake and a textured vegetable protein, is obtained by combining a source of microbial protein, which may contain up to 50% of milk protein, with a fat, in a weight ratio of 1:22 to 6:1.
Description
Th® invention relates to novel and useful textured vegetable protein food compositions wherein microbial proteins, certain derivatives and mixtures thereof with whey powder 1 / are advantageously employed.
There have been numerous publications in both the technical and patent literature dealing with methods of production of microbial cells for ·'· application in foods as well as processes for isolating protein-enriched fractions from these cells. By the terms microbial protein and microbial protein isolate as used herein is meant the protein-enriched fraction ob19 ' tained from disrupted cells of yeasts, bacteria and fungi which fraction has been treated such that it is relatively free of other cell components. Several methods have been described in the art for disruption of the cell walls of microorganisms to release cell components followed by isolation of the ’ > microbial protein released. These proteins have been recognized as being nutritious and their use in human food has been proposed.
U.S. 3,784,536 and U.S. 3,833,552 disclose methods of isolating microbial proteins by treatment of cells in aqueous or aqueous ethanolic medium containing mineral acid at a controlled temperature. The latter patent provides awater soluble whippable protein for food use.
-244072
U.S. Patent 3,121,080 provides .- process for extracting protein from microorganism cells which comprises rupturing the cells hy mechanical disintegration in a strongly alkaline medium and thereafter recovering the extracted proteins, U.S. Patent 3,343,222 discloses a process whereby an aqueous paste of microbial cells is heated while applying a shearing force to the hot paste, which is then, extruded to obtain a product which resists dispersion in water.
Yeast protein is produced by the method of t'.S. Patent 3,867,535 by separating Che soluble fraction obtained from ruptured yeast cells from the cull wail debris followed by hydrolysis of the nucleic acid with alkali at pH 9.5-12.5 ar.d 50-129’ ¢-, after which the protein is isolated by isoelectric precipitation. U.S, Patent 3,837,431 utilizes endogenous nuclease to hydrolyze nucleic acids present in alkaline solution after cells are ruptured; following this treatment the protein is precipitated.
In b',5, 3,891,772 a process is set forth for extraction of undesirable flavor and odor components from microbial cells by treatment in a slurry of aqueous alcohol containing 602 to 802 by volume of an alcohol having 1 to 3 carbon atoms, wherein the weight ratio of alcoholic solution to cells is in the range frcii: 3:1 to 7:1. The extracted cells are then recovered.
British. Patent 1,372,870 provides a method for improving the nutritional and functional properties of protein derived from unicellular microorganisms by maintaining an ammoniacal slurry of cells at 60° to 140° C. and at a pH of 8.0 to 11.0. The isolated product has reduced nucleic acid content.
In Japanese Patent 9,124,292, methods are described for extraction of protein from microbial cells. The cells are first defatted by an organic solvent, gel filtered to remove low molecular weight substances, the protein is extracted into aqueous alkali, then precipitated.
Japanese Patent 9,001,790 discloses a method by which microbial cells are heated at 80-220° C. under high pressure, greater than 10 atmospheres, of a gas containing more than 22% oxygen to improve the digestability of microbial protein. By the process of Japanese Patent 4,014,760 the extrac tion of protein from yeast cells is improved by homogenizing the cells in an 2 alkaline medium under a pressure above 100 kg./cm . A method for rupturing cells grown on hydrocarbon feed stock by autolysis is disclosed in U.S. 3,268,412 wherein autolysis is brought about by means oi enzymes contained in the microorganism or by addition of other enzymes.
Various methods for disrupting microbial cells and equipment used for this purpose are reviewed in Methods in Microbiology edited by Morris and Ribbons, Academic Press, Mew York, Ν. Y., 1971, Volume 5A, pp. 363-368; Volume 5B, pp. 1-54.
Compositions of demineralized dry whey solids and either monosodium phosphate or insoluble metaphosphate which exhibit functional properties ia food compositions are disclosed in U.S. 3,615,662, and comparable products employing alkali polyphosphates are provided by U.S. 3,620,757. Undenatured lactalburain phosphate food compositions wherein said phosphate derivative replaces a portion of the egg white normally contained is set forth in U.S. 3,706,575.
- 4 4407 /icetylated animal and vegetable proteins for food use are previously described in U.S. 3,619,206; U.S. 3,764,711; U.S. 3,782,971 and British Patent 1,294,664.
Summary of the Invention
While useful methods of isolation of microbial proteins suitable for use in human food are known in the art, the food compositions utilizing microbial proteins disclosed herein are novel, useful and surprisingly superior to their counterparts based entirely on conventional food protein sources
An object of the invention is to provide a food composition containing textured vegetable protein and a protein binding agent consisting of from 17 to 100% by dry weight of microbial protein and from 0 to 83% by dry weight of up to two additional ingredients selected from the group consisting of egg white, soy flour and wheat gluten.
Detailed Description of the Invention
The novel food compositions of the invention employ a microbial source of protein to replace from 17 to 100% by weight of certain protein-containing ingredients ordinarily used in such food compositions. The microbial sources of protein are especially effective in replacing vegetable proteins such as soy protein, wheat gluten, egg white, gelatin, proteinaceous foaming agents and milk protein sources such as nonfat dry milk, sodium caseinate, calcium caseinate and magnesium caseinate. In replacing these ordinary food proteins, the microbial source of protein can replace both the functional properties and the food value Of the conventional food proteins, i.e., the microbial source of protein serves as a functional protein and is nutritious.
By the term microbial source of protein, within the context of this invention, we mean microbial proteins as defined above, as well as certain metal salts of microbial proteins, derivatives of microbial proteins, denatured microbial proteins and mixtures of microbial protein and whey powder. Examples of metal salts of microbial proteins are the sodium, calcium and magnesium salts of microbial proteins. Examples of derivatives of the microbial proteins are the acetylated and ethanol treated derivatives of microbial proteins and the phosphate complexes of microbial proteins Examples of denatured microbial proteins are the heat denatured microbial proteins. Examples of mixtures of microbial protein and whey powder are those containing from up to 80% or more of whey powder and preferably about 20 to 80% of whey powder by weight; especially preferred are mix30 tures of microbial protein and whey powder containing about
50% whey powder by weight.
By the terra functional protein we mean proteins which primarily serve to improve the physical and/or organoleptic properties of a food, and their nutritive value may be of secondary importance in a particular food. Examples of physical and organoleptic properties of foods which are improved by a functional protein are water binding, fat binding, protein binding, emulsification, whippability, texture, volume, dispersibility, gelation, viscosity, flavor, aroma, color and the like. Examples of proteins known in the art and the functions they ordinarily improve in foods are egg albumen for whippability, color or as a binder of other proteins; egg yolk for emulsification, color or flavor; soy protein for water binding, fat binding, texture and whippability; gelatin for gelation; milk proteins and their salts for water binding, fat binding, flavor, texture; whippability, emulsification and heat stability; and wheat gluten for water binding, texture and flavor.
The microbial sources of protein of the invention have now been found to replace functional proteins known in the prior art such as the vegetable proteins, egg white, gelatin, edible proteinaceous foaming agents, milk protein and milk protein salts.
By the term edible proteinaceous foaming agents we mean commercially available edible proteins as well as edible mixtures containing proteins, or modified proteins and optionally containing other ingredients such as carbohydrates, chemically modified carbohydrates, salts and stabilisers, used as foaming and frothing agents in edible compositions such as marshmallow, whipped toppings, and in packaged bar mixes for alcoholic beverages such as wiskey sour and daiquiri mixes. Examples of such foaming agents are egg white and mixtures of modified or unmodified vegetable proteins with egg white, gelatin and gums.
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Examples of such foaming agents which are sold under tradenames are Hyfoma, a product of Lenderink and Co.,
Schiedam, the Netherlands, which is a mixture of vegetable proteins, egg white, sucrose and stabilizer; and Gunthers
Foaming Protein 1026 which is a mixture of modified soy protein and gelatin available from Α.Ξ. Staley Mfg. Co., Protein Division, Decatur, Illinois 62525.
The microbial sources of protein of the invention have now been found to replace the above-mentioned prior art ]_q functional proteins to provide superior food Compositions.
The microbial sources of protein disclosed herein have now been found to be surprisingly effective in their ability to function as fat binding and water binding agents. Accordingly, they have been found to be especially effective in fat con15 taining food compositions in which they replace at least a substantial portion of the conventional proteins used for their fat binding ability.
In referring to the food compositions of the invention the term source of protein refers to the microbial source of protein and the conventional food proteins being partially or completely replaced by the microbial source of protein. However, a given food composition may contain other food proteins or protein-containing ingredients not included in said source of protein.
Any microbial protein, and particularly those proteins isolated from microorganisms classified as yeasts, bacteria and fungi may serve to replace conventional proteins in the food compositions of the invention. By way of illustration, examples of genera of microorganisms suitable for providing microbial proteins are yeasts of the genera Saccharomyces, Candida, Hansenula and Pichia; bacteria of the genera Pseudomonas, Lactobacillus, Streptococcus, Micrococcus , Cellulomonas, Arthrobacter, Bacillus, Hydrogennomonas and Aerobacter; and fungi of the genera Trichoderma,
Fusarium, Penicillium, Aspergillus, Neurospora and Endomycopsis. Examples of species of microorganisms suitable for providing microbial proteins are listed in the following table:
Candida novallus Hydrogenomonas eucropha Endomycopis filberger
Preferred microbial proteins useful in the food compositions of the invention are those isolated from the yeasts Saccharomyces carlsbergensis, Saccharomyces cerevisiae. Saccharomyces fragilis and Candida utilis; the bacteria Pseudomonas methylotropha. Lactobacillus bulgaricus, Streptococcus lactis. Micrococcus ceriflcans and Cellulomonas cartalyticum; and the fungi Trlchoderma vlride, Fusarium solani, Penicillium chrysogenum, Aspergillus r.iger Aspergillus oryzae and Meurospora erasa.
The microbial proteins isolated after cell disruption may be further reacted to form certain derivatives which are also useful in many of the food compositions of the invention.
One such class of derivatives are the phosphate complexes which result when an aqueous solution or suspension of a microbial protein is contacted with an aqueous solution of an alkaline phosphate salt such as potassium metaphosphate, sodium hexametaphosphate, sodium polyphosphate, potassium polyphosphate, monosodium phosphate and mixtures thereof. Any of the above alkaline phosphate salts and mixtures of such salts may be contacted with any of the microbial proteins in varying proportions of phosphate salt to microbial protein, to provide microbial protein phosphate complexes which are useful in the food compositions of the invention. However, the preferred microbial protein phosphate complexes are those obtained by contacting, in aqueous solution, one part by weight of a mixture of sodium hexametaphosphate and potassium metaphosphate in a weight ratio from 6:1 to 10:1 with 10 to 15 parts by weight of microbial protein.
The phosphate complexes of the above microbial proteins are especially useful in whipped topping, coffee whitener, cake frosting, angel food cake and meringue topping food compositions.
Another useful class of derivatives of the above specified microbial proteins which serve as a microbial source of protein are the acetylated microbial proteins which are obtained when the microbial proteins are acetyla- ted to varying degrees of acetylation by methods known in the art for acetyla5 tion of proteins employing reagents such as acetic anhydride, acetyl chloride and acetyl bromide; see for example U.S. 3,619,206; U.S. 3,764,711 and U.S. 3,782,971. While any of the acetylated microbial proteins are useful in the food compositions of the invention, we prefer those obtained by carrying out the acetylation by dissolving one of the microbial proteins in water containing a polyvalent salt such as trisodium citrate which acts as a protein stabilizer. The resulting solution is then adjusted to a pH in the range of about 5 to 8 and treated with an acetylating agent such as acetic anhydride or acetyl chloride while maintaining the pH in the above specified range by periodic addition of strong alkali such as sodium hydroxide solution.
Especially preferred acetylated microbial proteins are those obtained by reacting microbial protein and acetic anhydride in a weight ratio of from about 1:1 to 1:0.1 at a temperature in the range of about 15° to 35° C.; an especially preferred range for the weight ratio of microbial protein and ace-i tic anhydride is from about 1:0.6 to 1:0.2.
The acetylated microbial proteins of the invention are especially useful in fat containing food compositions of the invention such as whipped toppings and coffee whiteners in which they display enhanced fat binding functionality.
Also included as a microbial source of protein within the scope of the present invention are mixtures of the above described microbial protein isolates with up to 80% or more of whey powder. Preferred mixtures are those con5 taining from 20 to 80% by weight of whey powder and especially said mixtures which contain about 50% whey powder by weight.
Whey powder is a readily available food ingredient commercially produced on a large scale from whole liquid whey by modern evaporation techniques. An illustrative and generally representive approximate composition of whey powder is:
Weight, %
Protein 12.5 Fat 1.0 Moisture 4.5 Ash 9.0 Lactose 73.0 100.0
For the purposes of this invention, whey powder of the above approximate composition or any of the specially treated whey powders such as demineralized whey powder, and whey protein concentrates obtained by techniques such as Ion exclusion, ultrafiltration, electrodialysis, reverse osmosis or .nzyroatic methods utilizing, e..£., lactase, are also suitable.
In many of the food compositions of the invention, the microbial protein-whey powder mixtures perform as well or better than the undiluted microbial proteins in replacing conventional food proteins. Said mixtures are especially useful in replacing whole milk powder and nonfat' dry milk in food compositions. Nonfat dry milk is also referred to herein as NFD!·!. In replacing· £.·£·> NFDM, they are ordinarily used to replace an equal weight of the conventional milk protein source. However, in certain cases they may be used in an amount approximately one-half to twice that of the protein being replaced to obtain superior food compositions.
The microbial protein-whey powder mixtures, which are also referred to herein as nonfat dry milk substitute, may be prepared by simply blending the two dry ingredients in the desired proportions. However, to insure intimate mixture of the components and to prevent separation due to differences in particle size of the components, It is preferred to blend them first in water by mixing followed by homogenization in a standard food homogenizer and pasteurization. The resulting mixture is then dried to a powder by standard drying techniques used in the food industry such as freeze drying, spray drying or vacuum drum drying.
Additionally, we have unexpectedly found that in food compositions containing textured vegetable protein and a protein binding agent, certain microbial proteins of the invention can effectively replace from 20 to 100% of the egg white, soy flour and wheat gluten ordinarily employed as protein binding agents.
In food compositions containing textured vegetable protein and a protein binding agent, such as, for example, in simulated meat products, the textured vegetable proteins are impregnated With a suitable binder, the impregnated veg5 etable proteins are then cooked to cause the binder to set to form a continuous mass that can be cut or shaped into pieces of suitable form.
While the above mentioned microbial proteins maybe employed advantageously as protein binding agents in
Ιθ food compositions containing any of the known textured vegetable proteins such as textured soy protein, textured wheat protein, textured peanut protein, textured cottonseed meal and the like, such food compositions wherein the textured vegetable protein is textured soy protein are preferred for reasons of economy and availability. Such food compositions are those containing textured vegetable protein and a protein binding agent consisting of from 17 to 100% by dry weight of microbial protein and from 0 to 83% by dry weight of up to two additional ingredients selected from the group consisting of egg white, soy flour and wheat gluten. Preferred microbial proteins for use as protein binding agents in the above food compositions are those microbial proteins isolated from the /casts S, fragilis, S_. earlsber gens is, S. cerevisiae and C. utilis; from the bacteria P. methylotropiia, L. buigaricus, S_. lactis, M. cerificans and C. cartalyticum; and from the fungi T. viride, F. solani, P. chrysogenum and A.
nifier.
The snack food industry has grown rapidly in recent years. The basic raw materials utilized include corn meal, wheat flour, potato flour, oat flour, tapioca and modified starches. These high starch foods can be fabricated into a wide variety of textures and shapes by extrusion methods. Extrusion is known to be a means of converting cereal products under controlled temperature and moisture conditions into expanded snack food products. Often, milk solids and soy protein are included to upgrade the nutritional quality and ;andling characteristics of the snack foods. The other major processing operation used to prepare snack foods is deep fat frying. Surprisingly, the microbial protein isolates described above can be used to replace soy protein, milk solids or both of these protein sources in snack food compositions to obtain products having acceptable taste and textural characteristics. In snack food compositions, mixtures of microbial proteins containing about 50% whey powder are also effective i:i replacing milk solids and NFDM.
The snack food compositions containing the microbial proteins of the invention cause less spattering during deep fat frying than those containing soy protein and milk solids, indicating that the microbial proteins are superior in binding water at frying temperatures. In addition, superior flavor and texture are observed in the snack food products of the invention.
Preparation 1
Microbial Protein Isolated by Mechanical Disruption
Candida utilis cells, 130 g. dry weight, were dispersed in 1000 ml.
of water and the pH adjusted to 11.5 by addition of IN NaOH. The cells 2 were homogenized at 633 Kg./cm . (9000 psi) at 30° C for one hour. The resulting mixture was centrifuged and the supemate decanted. The remaining solids were repulped in one liter of water and centrifuged. The supemates were combined, adjusted to pH 4.0 with IN hydrochloric acid and the precipitate
IQ collected by centrifugation. The solid product was washed with water, then suspended in water,· adjusted to pH 7.0 with sodium hydroxide solution and freeze dried to obtain 39 g. of protein isolate.
When the above process is repeated but using an equal weight of cells of Saccharomyces cerevisiae, Saccharomyces carlsbergensis, Saccharomyces fragilis, Aspergillus oryzae or Lactobacillus bulgaricus in place of C. utilis cells, the results are substantially the same.
When the above process is repeated but homogenization is carried out 2 at 200 Kg./cm. and 80° C. the results are essentially unchanged.
• When cells were homogenized at a pressure of 1000 Kg/cm. and. a temperature of 5° C. the result was essentially the same.
Preparation 2
Microbial Protein from Cells Disrupted by Treatment in Aqueous Acid
Saccharomvees fra?,ills. 500 g. dry weight, was suspended in 2.5 liters of normal hydrochloric acid to afford a slurrv of pH 1. The slurry was ι
i stirred while heating to 95° C. The mixture was then cooled to 25° C., adjusted.
I to pH 11.5 with sodium hydroxide solution and centrifuged. The supemate was ! !
decanted and the debris was repulped with one liter of water and centrifuged. :
The supernates were combined and adjusted to pH 4.0 with hydrochloric acid to !
t precipitate the protein. The protein was collected by centrifugation, repulped,' It in water and centrifuged again. The supernate was discarded and the solid f
.suspended in fresh water, adjusted to pH 7.0, centrifuged again and the solids dried in the vacuum oven at 65° C. to afford 115 g. of S_. fragilis protein.
When cells of Candida, utilis, £. lipolytics, £. pulcherima. Saccharomyces cerevisiae, £. carlsbergensis. Seurospora crasa, Aspergillus nlger, _A_. oryzae,. Penicllllum chrysogenum or Lactobacillus bulgarigus are used in place of S. fragllis cells the results are essentially unchanged.
When the above process is repeated by heating in 0.1 molar hydrochloric acid at 100° C. for 3 hours; heating in 5M sulfuric acid at 30° C. for 30 minutes or heating in 5M phosphoric acid at 70° C. for one minute, the
2' results are substantially unchanged.
Preparation 3
Isolation of Microbial Protein by Disrupting Cells in Aqueous Alkali
One hundred grams of dry Saccharomyces cerevisiae cells were sus5 pended in 500 ml. water and adjusted to pH 11.5 with aqueous potassium hydroxide solution. The mixture was stirred while heating at 85° C. for one hour. The mixture was then cooled to 25° C., centrifuged, and the supernate decanted. The residue was repulped in water (350 ml.) and recentrifuged. The combined supetnates were adjusted to pH 4.0 with dilute sulphuric acid and the resulting precipitate collected by centrifugation, repulped in water and isolated again by centrifugation. Tire solids were suspended in water, adjusted to pH 7.0 and freeze dried to obtain 16 grams of product.
Khen the process is repeated:
a. with Candida titilis cells at pH 12 and at a temperature of
° C. for 15 hours;
b. with S_. carlsbergensis cells at pH 8 and 100° C. for 5 ' hours;
c. with Streptococcus lactis cells at pH 12, 100° C. for one hour;
d. with Trichoderma vlride cells at pH 11 and 90° C. for two hours;
e. with Cellumonas cartalyticum cells at pH 12 and 80° C. for 3 hours;
f. with Penicillium chrysogenum cells at pK 11.5 and 85° C. for two hours;
g·· with Aspergillus oryzae cells at pH 11.5 and 90° C. for two hours; the results are substantially the same.
- 2044072
Preparation 4
Microbial Protein from Cells Disrupted by Autolysis
Candida utilis cells, 350 g. dry weight were suspended in 1500 ml. water and adjusted to pK 5.0. The slurry was stirred at 50° C. for 90 hours.
The resulting mixture was cooled to 30°C., adjusted to pH 11.5 with aqueous potassium hydroxide solution and centrifuged at 12,000 r.p.m. for 10 minutes. The supernate was decanted and the cell debris washed with water (one liter) and recentrifuged. The combined supernates were adjusted to pH 4.0 and diluted with an equal volume of 95% ethanol. The precipitated protein was collected by centrifugation and washed with an equal volume of water. The solids were suspended in water, adjusted to pH 7.0, and freeze dried to obtain
g. of protein isolate.
When the above procedure is repeated, but using cells of one of the following yeasts, fungi or bacteria in place of C. utilis cells the results are substantially unchanged.
w 1 otropha 3 u rt ft rt w rt ! o rt jj uin rt rt bC ft S rt (Λ rt , rt U rt ft * rt rt A 3 « rt Φ o rt ft ft A rt JJ A « «Γ rt Φ y ft u rt ft y S3 W Oi rt « ft A 3 3 u M 4) φ w w rt U y ft ft « 3 a rt y ω e U tl U rt ‘ri 0 n tt rt w y § y 0 e « eg A 3 o rt 0 □ 3 Q rt u 0 λ ft H rt ft rt 0 *3 '0 A 3 rt A rt ft 9 ft 0) rt rt ft y y Φ u ft rt U ft rt 5 W tt ft 41 tt 4 eg A rt M O A3
g.
rt tt ft tt
P >Φ.
ft a;
Preparation 5
Microbial Protein from Cells Disrupted by Extrusion
A wet paste, 1000 g., of Saccharomyces fragilis cells (650 g. dry weight) at pH 11.0 and moisture content of 35% was extruded using a
Wenger extruder, (Laboratory Model, length to diam. ratio, 12:1). The extrusion was carried out at 120° C. and at a maximum pressure of 35 Kg./cm. Excellent cell disruption is noted upon examination under the microscope.
The extruded material was then dissolved in water ac pH 11.5. The debris was removed by centrifugation and washed with water. The protein In the combined supernatea was precipitated by isoelectric precipitation at pH 3.5-4.5, washed with water and dried in the vacuum oven at 70° C. to obtain 78 g. of product which assayed 87% protein (Ν x 6.25).
When the above procedure is repeated with Candida utilis cells and extruding at a temperature of 80° C. and at a maximum pressure of 200 kg./cm.
the results are substantially the same. Alternatively, the process is also carried out with equal facility using 3.. cervisiae cells at 300° C. and kg./cm.*-.
When either of the above processes are carried out with Aspergillus niger, A. oryzae, Micrococcus, cerlflcans, 3.. carlsbergensis, L. bulgaricus,
S. lactis, Fusarium solanl. or Trichodsrca viride cells in place of 3_. fragilis calls, the results are essentially the same.
4072
Preparation 6
Disruption of Cells by Treatment at High Temperatures and Pressure
Ten liters of a 52 by weight slurry of S_. fragilis cells are heated in an autoclave at 150-160° C. and at a pressure of 50-80 p.s.i. (3.8-6.1 2 kg./cm ) for six hours. The autoclave is allowed to cool to room temperature overnight after which the contents are adjusted to pH 11 with potassium hydroxide solution and centrifuged. The supernate is decanted and the remain ing solids repulped in 5 liters of water and centrifuged. The supernates are combined, adjusted to pH 4.0 with hydrochloric acid and the precipitate is collected by centrifugation. The solid product is washed with water, then suspended in water and adjusted to pH 7.0 with potassium hydroxide solution. The solid protein is obtained by spray drying.
When the above process is repeated but employing a temperature of
60° C. for 20 hours or a temperature of 200° C. for 2 hours, the results are substantially unchanged.
If S. fragilis cells are replaced by cells of the yeasts, fungi or bacteria listed below the results are essentially unchanged.
4407a
Ye is I
C. util is
C. t i po1ylica
C. subtropacal i s 5 C_. guilliernondi
Hansenula pc lymorpha
C_. novellus
A.· fragilis
S. cerevisiae _S_. carlsbergensis
Pichla pastoris
Pichia mlso/magi
3.1 ter i a
Pseudomonas meihy l ot roplia
Lactob-iciJ lin; bulg.iricis
Streptococcus lac Lis
Micrococcus ceriflcans
Cellulomonas cartalyticum
Cellulobacillus myxogenes
Fungi l'r ichndenna viride
Fusarium solani
Penicil Hum chrysogenum
Aspergillus niger
A. oryaae
Meurospora crasa
Preparation 7
To a 2% suspension of Micrococcus ,'cerificans cells is added sufficient concentrated sulfuric acid to make the suspension 0.2M with respect to HnSO^. The resulting mixture is heated at 70° C. for 30 minutes then cooled and adjusted to pH 11 with sodium hydroxide solution. This solution is homogenised by means of a EIBI cell disintegrator under a pressure of o
600 Kg./cmt and worked up as described in Example 1.
Preparation 8
Candida utilis cells, 350 g. dry weight are suspended in 1500 ml.
of water and adjusted to pH 5.0. The slurry is autolyzed at 50° C. for 90 hours then homogenized and worked up as described in Example 1.
Preparation 9
Microbial Protein-Phosphate Complex
Twenty-five grains of £. utilis protein was added to 500 ml. of water and the mixture warmed to effect solution. To the warm solution was then added 20 ml. of a solution containing 1.78 g. of sodium hexametaphosphate and 0.22 g. of potassium metaphosphate. The resulting mixture was stirred while allowing to cool to room temperature then centrifuged to remove the precipitated phosphate complex; yield, 26 g.
When the above is repeated with 20 g. of £. fragilis protein or
g. of P_. methylotropha protein in place of the 25 g. of _C. utilis protein, the results are substantially unchanged.
When the above procedure employing 25 g. of £. utilis protein is repeated but employing a total of 2.0 g. of sodium hexametaphosphate and potassium metaphosphate in weight ratios of 6:1 and 10:1 the results are essentially the same.
Preparation 10
Ethanol Treatment of Microbial Protein Isolates
A. One hundred grams of dry microbial protein isolate of Example 4 and 750 ml. of 95% (by volume) ethanol are stirred at 30° C. for one hour then centrifuged. The solids are slurried again with a fresh portion of 95% ethanol, centrifuged and the solids dried in the vacuum oven at 50° C. overnight. The ethanol treated protein is judged to have an improved flavor quality, devoid of bitterness and exhibited improved functional properties in certain food applications such as in whipped toppings.
When the above procedure is carried out using 20% to 100% ethanol (by volume) in place of 95% ethanol or at temperatures of 20° C. or 60° C. a significant improvement in protein flavor is noted in each case.
When any of the protein products of the preceding examples are treated by the above procedure, a definite improvement in flavor quality and/or functional properties of the alcohol treated protein is noted.
. Candida utilis cells, 130 g. dry weight, are dispersed in
1000 ml. of water and the pH adjusted to 11.5 by addition of IN NaOH. The o cells are homogenized at 633 Kg./cm? (9000 psi) at 30° C. for one hour. The resulting mixture ig centrifuged and the supernate decanted. The remaining solids are repulped in one liter of water and centrifuged. The supernates are combined, adjusted to pH 4.0 with IN hydrochloric acid and the precipitate collected by centrifugation. The solid product is washed with water, then resuspended in 100 ml. of water. To the slurry 400 ml. of pure ethanol is added and the resulting mixture warmed to 30° C. and stirred for one hour at this temperature. The mixture is then cooled, centrifuged and the solid product is washed with water, then suspended in water, adjusted to pK 7.0 and freeze dried.
Preparation 11
Acetylated Microbial Protein
A. A suspension of 50 grans of the £. utilis protein isolate of Exanple 3 in 1000 ml. of water was adjusted to pH 5.7, 10 g. of trisodium citrate was added and the mixture stirred for 30 minutes. The resulting solution was adjusted to pH 7.0 with IN sodium hydroxide and 30 g. of acetic anhydride was added dropwise over a 60 minute period while maintaining the reaction mixture at pH 7-8 by periodic addition of sodium hydroxide (IN).
The reaction mixture was stirred at room temperature for one hour after the addition, then stored at 20° C. for use on an as-is basis. If desired the ί-olid product can be isolated by conventional methods such as lyophilization.
B. When the above procedure is repeated, but using 50 g. of S_. cerevisiae protein in place of £. utilis protein and 10 g. of acetic anhydride., an acetylated protein with commensurately lower degree of acetylation is obtained.
Preparation 12
Non-Pat Dry Milk Substitute
A. £, utilis protein isolated of Exanple 1, 100 g., and an equal weight of whey powder were blended by mixing in 1000 ml. of water at pH 7.0.
The resulting mixture was then homogenized at 2000 psi, pasteurized, and concentrated to a paste. The paste was then freeze-dried.
B. fraeilis protein isolate of Example 2, 40 g., and whey powder, 160 g., were blended by mixing in 1000 ml. of water at pH 7.0. The resulting mixture was then treated as described in Part A. above, to obtain a mixture cor.taining 20% microbial protein and 80% whey powder.
C. §.· fra gills protein isolate of Example 5, 160 g., and whey powder, 40 g., were blended by mixing in 1000 ml. of water at pH 7.0. The resulting mixture was then treated as described in Part A, above, to obtain a mixture containing 80% microbial protein isolate and 20% whey powder.
4 0 7 2
Example 1
Microbial Protein as a Replacement for Egg White as a Protein Binding Agent
A typical simulated food product in which egg white is successful replaced by the microbial proteins of the invention as a protein binder is set forth below in which soy protein fibers, 100 g., containing 60-652 of water (by weight) are impregnated with the following ingredients:
Ingredients Control Test Dried egg white 20.0 g. __
Microbial protein — 20.0 g. Flour 10.0 g. 10.0 g. Nonfat milk solids 10.0 g. 10.0 g. Sodium chloride 8.0 g. 8.0 g. Yellow onion powder 1.0 g. 1.0 g. 15 Monosodium glutamate 0.5 g. 0.5 g. Red Dye (22 in water) 1.5 ml. 1.5 ml Water 150.0 ml. 150.0 ml
Tie impregnated fibers are baked at 350° F. (177° C.) for 20 minutes, cooled and cut into squares to afford the final product. Coon evaluation, the test product is found to have superior texture and flavor.
S. fragilis protein, cere.visiae protein and 5., lactis protein are especially effective in this use.
Example 2
Another simulated food product based on soy protein fibers which demonstrates the superiority of the microbial proteins of the invention as protein binding agents is prepared according to the following formulation and procedure.
Ingredients
Parts by Weight
Vegetable oil 50 Glyceryl lactopalmitate 4 Rater (hot) 160 Monosodium glutamate 3 Yellow onion powder 18 3rown sugar 7 Red dye (1% aqueous solution) 6 Egg white, dried or microbial protein 10 Toasted, defatted soybean flour (200 mesh) 20 Fresh gluten (33% solids by weight) 90 Sodium chloride 25 Water 40
The soy protein fiber (35-40% solids by weight),
100 parts, is impregnated with 200 parts of an emulsion of the above ingredients. The emulsion is prepared by first mixing the vegetable oil, hot water, glyceryl lactopalmitate,MSG, onion powder, sugar and dye. In the 40 g. portion of cold water containing the salt are dispersed the dried egg white or microbial protein isolate of Example 2, soybean flour and gluten. This dispersion is then added to the other ingredients with high speed stirring to form a free flowing emulsion,
Tlie impregnated soy protein fibers are heated at 340° F. (171° C.) for 30 minutes, cooled and cut Into strips.
EXAMPLE 3
Microbial Protein as a Binding .Agent for Textured Protein
Meat patties containing one of the microbial proteins of the invention as a binding agent for textured protein, water and fat were prepared using the following formulations and procedure.
Weight, Grams
Test Patties
Ingredients Control As c D Hydrated TVP + 100 100 ICO 100 100 Vegetable fat 20 20 20 20 20 Dried egg white 5 — 5 — Microbial Protein* -- 5 -- 5 5 Soy flour 10 10 Microbial Protein* — — 10 10 10 Wheat gluten 10 10 10 — — Microbial Protein* — — 10 — Water 25 25 25 25 25 Total 170 170 170 170 160
* £. fragilis protein * Hydrated textured vegetable protein (TVP) is prepared by blending the following ingredients and allowing to stand overnight.
Ingredients Weight, Grams
Meat flavor 25.0
Monosodiura glutamate 3.C
Sodium chloride 12.5
Water 300.0
White pepper 0.3
Textured vegetable protein, dry 125.0
471.0
4 073
Example 3 (Continued)
Procedure
Melt the vegetable fat in a beaker and add the water mix in the appropriate prot.ein binders (i.e., egg white, gluten, flour, microbial protein) and stir for 5 minutes. Blend the above mixture with the 100 g. of hydrated TV? and allow to stand for 1-3 hours.
Shape into patties and broil in oven at 375“ F. (190° C.) for 15 minutes. The patties are then evaluated for functional and sensory properties.
: Meat Patties Total Grams of Protein Binders (Gram Microbial Protein) Water and Fat Loss on Cooking, % Sensory . Evaluation T Control 25 (0) 19.7 5.0 Test A 25 (5) 16.1 4.5 15 Test B 25 (10) 15.1 5.0 Test C 25 (25) 12.2 5.0 Test D 15 (15) 13.4 4.5 , ^Includes ι color, texture, mouthfeel and taste properties.
Evaluated on arbitrary scale range from 1 for very poor to 5 for excellent.
Thus, the microbial protein shows good protein binding characteristic when compared with egg white, soy flour and wheat gluten. The loss of fat and water upon cooking the meat patties decreases directly with increased amounts of microbial protein.
When other microbial proteins of the invention isolated from cells of the following yeasts, bacteria and fungi are employed in the above procedure in place of the S.. fragilis protein, similar results are obtained.
leasts
S_. carbergen30 sis
J3. cerevisiae
C. utilis
Bacteria ’ Fungi P. methylotropha T. viride L. buigaricus F. solani S. lactis P. chrysogenum M. cerificans A. niger C. cartalyticum
Claims (6)
1. CLAIMS:1. A food composition containing textured vegetable protein and a protein binding agent said binding agent consisting of from 17 to 100% by dry weight of microbial protein 5 and from 0 to 83% by dry weight of up to two additional ingredients selected from the group consisting of egg white, soy flour and wheat gluten.
2. Food compositions according to Claim 1 wherein said vegetable protein is soy protein. IO
3. Food compositions according to Claim 1 wherein said microbial protein is isolated from a yeast selected from the group consisting of S.fragilis, S. carIsbergenis, S. cerevisiae, and C. utilis.
4. Food compositions according to Claim 1 wherein said 15 microbial protein is isolated from a bacterium selected from the group consisting of P. methylotropha, L. bulgaricus, S. lactis, M. cereficans and C. cartalyticum.
5. Food compositions according to Claim 1 wherein said microbial protein is isolated from a fungus selected from the 2o group consisting of T. viride, F. solani, P. chrysogenum and A. niger.
6. A food composition according to any one of Claims 1 to 5, and substantially as hereinbefore described in any one of Examples 1 to 3.
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US65912376A | 1976-02-18 | 1976-02-18 |
Publications (2)
Publication Number | Publication Date |
---|---|
IE44072L IE44072L (en) | 1977-08-18 |
IE44072B1 true IE44072B1 (en) | 1981-08-12 |
Family
ID=24644135
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
IE2430/76A IE44072B1 (en) | 1976-02-18 | 1976-11-01 | Novel food compositions containing microbial proteins |
Country Status (14)
Country | Link |
---|---|
JP (1) | JPS52102444A (en) |
AR (2) | AR218443A1 (en) |
AU (1) | AU504076B2 (en) |
BE (1) | BE851561A (en) |
CA (1) | CA1094866A (en) |
CH (1) | CH621244A5 (en) |
DE (1) | DE2651464A1 (en) |
FR (2) | FR2365968A1 (en) |
GB (1) | GB1556297A (en) |
IE (1) | IE44072B1 (en) |
IT (1) | IT1086666B (en) |
LU (1) | LU76796A1 (en) |
NL (1) | NL7701679A (en) |
SE (1) | SE7701800L (en) |
Families Citing this family (27)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS57118755A (en) * | 1981-01-16 | 1982-07-23 | Nippon Suisan Kaisha Ltd | Production of food products containing emulsified fat |
US4335155A (en) * | 1981-03-06 | 1982-06-15 | General Mills, Inc. | Composition for aerated frozen desserts containing fruit puree and method of preparation |
DE3313644A1 (en) * | 1983-04-15 | 1984-10-18 | Hoechst Ag, 6230 Frankfurt | COFFEE WHITENER |
US4904485A (en) * | 1986-10-02 | 1990-02-27 | Kanegafuchi Kagaku Kogyo Kabushiki Kaisha | Fat compositions suitable for use in bakeries or confectioneries |
EP0347237B1 (en) * | 1988-06-16 | 1994-04-20 | Unilever Plc | Edible plastic compostitions |
DE9107764U1 (en) * | 1991-03-18 | 1992-10-22 | Voag, Josef, Dipl.-Ing., 80333 München | pudding |
GB0110954D0 (en) | 2001-05-04 | 2001-06-27 | Marlow Foods Ltd | Edible fungi |
GB0110953D0 (en) * | 2001-05-04 | 2001-06-27 | Marlow Foods Ltd | Edible fungi |
CA2575319C (en) * | 2004-07-27 | 2014-10-14 | Unilever Plc | Aerated food products containing hydrophobin |
EP1926399B2 (en) * | 2005-09-23 | 2014-03-12 | Unilever PLC | Process for producing a frozen aerated composition |
ATE417511T1 (en) | 2005-09-23 | 2009-01-15 | Unilever Nv | AERATED PRODUCTS WITH LOW PH VALUE |
EP1926398B1 (en) | 2005-09-23 | 2011-01-05 | Unilever PLC | Aerated products with reduced creaming |
GB2432772B (en) * | 2005-11-30 | 2011-06-01 | Sis | Improvements in and relating to nutritional products |
DE602005006829D1 (en) | 2005-12-21 | 2008-06-26 | Unilever Nv | Frozen aerated desserts |
AU2007211713B2 (en) * | 2006-01-31 | 2011-09-01 | Unilever Plc | Aerated compositions comprising hydrophobin |
EP2358743B1 (en) | 2008-12-16 | 2012-10-10 | Unilever PLC | Method for extracting hydrophobin from a solution |
US8357420B2 (en) | 2009-05-29 | 2013-01-22 | Conopco, Inc. | Oil-in-water emulsion |
US8394444B2 (en) | 2009-05-29 | 2013-03-12 | Conopco, Inc. | Oil-in-water emulsion |
EP2347658A1 (en) * | 2010-01-20 | 2011-07-27 | Nestec S.A. | Oil gel |
CA3034678A1 (en) | 2016-08-25 | 2018-03-01 | Perfect Day, Inc. | Food products comprising milk proteins and non-animal proteins, and methods of producing the same |
US11051532B2 (en) | 2017-09-22 | 2021-07-06 | Impossible Foods Inc. | Methods for purifying protein |
JP2023511931A (en) * | 2020-01-21 | 2023-03-23 | ベーリンガー インゲルハイム フェトメディカ ゲーエムベーハー | Effervescent foam for delivery of functional ingredients |
US12011016B2 (en) * | 2020-09-14 | 2024-06-18 | Impossible Foods Inc. | Protein methods and compositions |
CA3212363A1 (en) * | 2021-03-01 | 2022-09-09 | Impossible Foods Inc. | Materials and methods for protein production |
CN114836331B (en) * | 2022-04-26 | 2023-04-25 | 内蒙古工业大学 | Candida utilis and application thereof |
WO2024100280A1 (en) * | 2022-11-10 | 2024-05-16 | Arbiom Sas | Formulations for high-protein, non-dairy cheese analog |
CN117481250A (en) * | 2023-12-29 | 2024-02-02 | 北京幸福能量健康科技有限公司 | Yeast protein composition capable of replacing whey protein, preparation method and application |
-
1976
- 1976-11-01 IE IE2430/76A patent/IE44072B1/en unknown
- 1976-11-11 DE DE19762651464 patent/DE2651464A1/en active Pending
-
1977
- 1977-02-17 GB GB6744/77A patent/GB1556297A/en not_active Expired
- 1977-02-17 FR FR7704557A patent/FR2365968A1/en active Granted
- 1977-02-17 CH CH200877A patent/CH621244A5/en not_active IP Right Cessation
- 1977-02-17 AR AR266578A patent/AR218443A1/en active
- 1977-02-17 BE BE1007953A patent/BE851561A/en unknown
- 1977-02-17 SE SE7701800A patent/SE7701800L/en unknown
- 1977-02-17 IT IT48073/77A patent/IT1086666B/en active
- 1977-02-17 CA CA271,999A patent/CA1094866A/en not_active Expired
- 1977-02-17 JP JP1666977A patent/JPS52102444A/en active Pending
- 1977-02-17 NL NL7701679A patent/NL7701679A/en not_active Application Discontinuation
- 1977-02-17 AU AU22400/77A patent/AU504076B2/en not_active Expired
- 1977-02-17 LU LU76796A patent/LU76796A1/xx unknown
- 1977-10-05 FR FR7729981A patent/FR2365964A1/en active Granted
- 1977-10-07 AR AR269498A patent/AR214092A1/en active
Also Published As
Publication number | Publication date |
---|---|
FR2365968A1 (en) | 1978-04-28 |
DE2651464A1 (en) | 1977-08-25 |
FR2365964A1 (en) | 1978-04-28 |
GB1556297A (en) | 1979-11-21 |
NL7701679A (en) | 1977-08-22 |
AU504076B2 (en) | 1979-10-04 |
AU2240077A (en) | 1978-08-24 |
SE7701800L (en) | 1977-10-03 |
FR2365968B1 (en) | 1981-08-28 |
BE851561A (en) | 1977-08-17 |
LU76796A1 (en) | 1978-10-18 |
AR218443A1 (en) | 1980-06-13 |
CA1094866A (en) | 1981-02-03 |
JPS52102444A (en) | 1977-08-27 |
FR2365964B1 (en) | 1981-06-26 |
IE44072L (en) | 1977-08-18 |
AR214092A1 (en) | 1979-04-30 |
IT1086666B (en) | 1985-05-28 |
CH621244A5 (en) | 1981-01-30 |
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