EP1942751A1 - Verfahren zur reduktion von acrylamid in gegarten nahrungsmitteln - Google Patents
Verfahren zur reduktion von acrylamid in gegarten nahrungsmittelnInfo
- Publication number
- EP1942751A1 EP1942751A1 EP06804040A EP06804040A EP1942751A1 EP 1942751 A1 EP1942751 A1 EP 1942751A1 EP 06804040 A EP06804040 A EP 06804040A EP 06804040 A EP06804040 A EP 06804040A EP 1942751 A1 EP1942751 A1 EP 1942751A1
- Authority
- EP
- European Patent Office
- Prior art keywords
- protein
- peptide composition
- food
- uncooked food
- composition
- 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.)
- Withdrawn
Links
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
- A23L3/00—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs
- A23L3/34—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals
- A23L3/3454—Preservation of foods or foodstuffs, in general, e.g. pasteurising, sterilising, specially adapted for foods or foodstuffs by treatment with chemicals in the form of liquids or solids
- A23L3/3463—Organic compounds; Microorganisms; Enzymes
- A23L3/3526—Organic compounds containing nitrogen
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23B—PRESERVING, e.g. BY CANNING, MEAT, FISH, EGGS, FRUIT, VEGETABLES, EDIBLE SEEDS; CHEMICAL RIPENING OF FRUIT OR VEGETABLES; THE PRESERVED, RIPENED, OR CANNED PRODUCTS
- A23B7/00—Preservation or chemical ripening of fruit or vegetables
- A23B7/14—Preserving or ripening with chemicals not covered by groups A23B7/08 or A23B7/10
- A23B7/153—Preserving or ripening with chemicals not covered by groups A23B7/08 or A23B7/10 in the form of liquids or solids
- A23B7/154—Organic compounds; Microorganisms; Enzymes
-
- 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
- A23L19/00—Products from fruits or vegetables; Preparation or treatment thereof
- A23L19/10—Products from fruits or vegetables; Preparation or treatment thereof of tuberous or like starch containing root crops
- A23L19/12—Products from fruits or vegetables; Preparation or treatment thereof of tuberous or like starch containing root crops of potatoes
-
- 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
- A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
- A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
-
- 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
- A23L5/00—Preparation or treatment of foods or foodstuffs, in general; Food or foodstuffs obtained thereby; Materials therefor
- A23L5/20—Removal of unwanted matter, e.g. deodorisation or detoxification
- A23L5/27—Removal of unwanted matter, e.g. deodorisation or detoxification by chemical treatment, by adsorption or by absorption
Definitions
- This invention relates to a process for reducing acrylamide formation in cooked food. More particularly, this invention relates to a process for reducing acrylamide formation in cooked food containing asparagine.
- acrylamide is formed in cooked food when heated to a temperature that supports the reaction of asparagine and reducing sugars (aldose) present in the food.
- the reaction involved is known as a Maillard reaction and involves the condensation of asparagine and reducing sugars in the food to form acrylamide.
- the reaction is effected at about 140° and above.
- acrylamide may cause cancer in animals.
- Representative foods containing asparagine and reducing sugars include potatoes, such as french fried potatoes, potato chips, corn based chips, taco shells and breakfast cereals.
- uncooked food containing asparagines and reducing sugars to be cooked is coated, injected and/or admixed with a dry protein mixture or an aqueous acidic solution of protein mixture derived from animal muscle tissue and/or with a peptide composition derived from the mixture or from the aqueous acidic solution of protein mixture in order to reduce acrylamide formation in the food during cooking at a temperature above about 14O 0 C.
- the protein mixtures comprise a mixture of myofibrillar proteins and sarcoplasmic proteins obtained by one of the processes disclosed in U.S. Patents 6,005,073; 6,288,216; 6,136,959 and/or 6,451 ,975 all of which are incorporated herein by reference in their entirety.
- dry protein mixture as used herein is meant a dehydrated, protein mixture of myofibrillar proteins and sarcoplasmic proteins derived from animal muscle tissue and which is obtained from an aqueous acid solution (less than or equal to pH 4.0) or an aqueous alkaline solution (greater than or equal to pH 10.5).
- the dry protein mixture also contains less than about 15 weight percent water, preferably between about 3 and 10 weight percent water and most preferably between about 3 and 7 weight percent water based on the total weight of the protein mixture and water. While a dry protein mixture containing 0% water is useful in the present invention, dry powders, in general, containing 0 to 3 weight percent water can be dangerous to process on a commercial scale. Solid mixtures of myofibrillar proteins and sarcoplasmic proteins containing greater than about 15 weight percent water based on total weight of the protein mixture and water are undesirable in this invention since they are microbially unsound.
- aqueous acidic protein solution an aqueous solution of myofibrillar proteins and sarcoplasmic proteins derived from animal muscle tissue and having a pH of 4.0 or less, preferably pH 3.5 or less and most preferably between about 2.5 and about 3.5, but not so low as to adversely affect the protein functionality.
- the aqueous acidic protein solution can be obtained directly from animal muscle tissue by the processes described below or by dissolving the dry protein mixture in water or in a pharmaceutically or food grade acceptable aqueous acidic solution.
- aqueous alkaline protein solution as used herein is meant an aqueous solution of myofibrillar proteins and sarcoplasmic proteins having a pH from about 10.5 to about 12.0.
- the aqueous alkaline protein solution can be obtained directly from animal muscle tissue by the process described below.
- a dry alkaline protein mixture is obtained by drying the aqueous alkaline protein solution such as by lyophilization, evaporation or spray drying.
- the dry protein mixture or dry alkaline protein mixture of myofibrillar proteins and sarcoplasmic protein, in powder form, dehydrated form or small particulate form or peptide composition derived from the dry protein mixture is applied to the surface of the food to be cooked, is injected into the food to be cooked and/or is mixed with the food (ground, minced or thinly sliced) to be cooked such as hamburger or sausage.
- the aqueous acidic protein solution or aqueous alkaline protein solution or peptide composition derived from the aqueous acidic protein solution or aqueous alkaline protein solution can be applied to the surface of the food or it can be mixed with the food or it can be injected into the food.
- the food containing the dry protein mixture, dry alkaline protein mixture, aqueous alkaline protein solution or aqueous acidic protein solution or peptide composition derived therefrom then can be cooked such as by baking or frying such as by deep fat frying at a temperature above about 14O 0 C up to a temperature where the food is overcooked reducing acrylamide formation in the food.
- the difference in weight of acrylamide treated in accordance with this invention after being cooked in compared with food without the dry protein mixture or aqueous acidic protein solution or peptide composition derived therefrom after being cooked in is between about 25 and about 95 %, preferably, between about 50 and about 95% less acrylamide.
- the dry alkaline protein mixture of myofibrillar proteins and sarcoplasmic protein, in powder form, dehydrated form or small particulate form or peptide composition derived from the dry alkaline protein mixture is applied to the surface of the food to be cooked, is injected into the food to be cooked, is injected into the food to be cooked and/or is mixed with the food (ground, minced or thinly sliced) to be cooked such as hamburger or sausage.
- the aqueous alkaline protein solution or peptide composition derived from the aqueous alkaline protein solution can be applied to the surface of the food or it can be mixed with the food or it can be injected into the food.
- the food containing the dry protein mixture or aqueous alkaline protein solution or peptide composition derived therefrom then can be cooked at elevated temperature above about 14O 0 C while minimizing formation of acrylamide.
- the difference in acrylamide formation between food treated in accordance with this invention after being cooked compared with food without the dry alkaline protein mixture or aqueous alkaline protein solution or peptide composition derived therefrom after being cooked is between about 25 and about 95 %, preferably, between about 50 and about 95% less acrylamide.
- the peptide composition useful in the present invention is obtained by contacting the dry protein mixture, the aqueous acidic protein solution; the aqueous alkaline protein solution or the dry alkaline protein mixture with an enzyme composition which converts the protein to a peptide composition at the pH of the protein.
- the peptide composition can be a dry peptide composition, an aqueous acidic peptide composition, an aqueous alkaline peptide solution or a dry alkaline peptide mixture.
- food containing asparagine and reducing sugars to be cooked at above about 14O 0 C is coated, injected with and/or admixed with a dry protein mixture, a dry alkaline protein mixture, an aqueous acidic protein solution or an aqueous alkaline protein solution of myofibrillar proteins and sarcoplasmic proteins derived from animal muscle tissue and/or a peptide composition derived from the dry protein mixture, the dry alkaline protein mixture, the aqueous acidic protein solution or the aqueous alkaline protein solution.
- the dry protein mixture, dry protein alkaline mixture, aqueous alkaline protein solution and aqueous acidic protein solution are obtained by the processes disclosed in U.S. Patents 6,005,073, 6,288,216, 6,136,959 and 6,451,975 all of which are incorporated herein by reference in their entirety.
- the peptide composition utilized in the present invention is obtained by contacting the dry protein mixture, the aqueous acidic protein solution, the dry alkaline protein mixture or an aqueous alkaline protein solution with an enzyme that converts the protein to a peptide. This dry protein mixture is obtained by one of four processes.
- animal muscle tissue is formed into small tissue particles which are then mixed with sufficient acid to form a solution of the tissue having a pH of 4.0 or less, preferably 3.5 or less and most preferably between about 2.5 and about 3.5, but not such a low pH as to adversely modify the animal tissue protein.
- the solution is centrifuged to form a lowest membrane lipid layer, an intermediate layer of aqueous acidic protein solution and a top layer of neutral lipids (fats and oils).
- the intermediate layer of aqueous acidic protein solution then is separated from the membrane lipid layer or from both the membrane lipid layer and the neutral lipid layer.
- the protein mixture is free of myofibrils and sarcomeres.
- the protein in the aqueous acidic protein solution is recovered after centrifugation (when used) or by drying the aqueous acidic solution, such as by evaporation, spray drying or lyophilization to form the dry protein mixture having the low pH it had when it was dissolved in the aqueous acidic protein solution.
- the aqueous acidic protein solution can be utilized with the uncooked food without drying the solution.
- the protein in the aqueous acidic protein solution can be precipitated and recovered and mixed with a pharmaceutically acceptable or food grade acid to form an aqueous acidic protein solution of a desired viscosity.
- the proteins in the acidic protein solution can be raised to a pH between about 10.5 and 12 using base to form an aqueous alkaline protein solution.
- animal muscle tissue is formed into small tissue particles which are then mixed with sufficient aqueous base solution to form a solution of the tissue wherein at least 75% of the animal muscle protein is solubilized, but not such a high pH as to adversely modify the animal tissue protein, i.e., a pH between about 10.5 and about 12.
- the solution is centrifuged to form a lowest membrane lipid layer, an intermediate aqueous protein rich layer and a top layer of neutral lipids (fats and oils).
- the intermediate aqueous alkaline protein-rich layer then is separated from the membrane lipid layer or from both the membrane lipid layer and the neutral lipid layer.
- aqueous alkaline protein solution can be recovered at this point.
- the pH of the protein-rich aqueous phase can be lowered to a pH below about 4.0, preferably below about 3.5 and most preferably between about 2.0 and 3.5 to form the aqueous acidic protein solution.
- the protein in the aqueous acidic protein solution is recovered after centrifugation (when used) by drying the aqueous acidic protein solution, such as by evaporation, spray drying or lyophilization to form a powder product having the low pH it had when it was dissolved in the aqueous acidic solution.
- the aqueous acidic protein solution can be applied directly to the food without drying.
- the protein in aqueous alkaline solution having a pH between about 10.5 and 12.0 recovered after centrifugation (when used) can be dried, such as by spray drying, evaporation or lyophilization to form a powder product.
- the dry protein mixture, the dry alkaline protein mixture, the aqueous acidic protein solution or the aqueous alkaline protein solution then is coated or injected into and/or admixed with the uncooked food.
- the dry protein mixture, dry alkaline protein mixture, aqueous acidic protein solution, or aqueous acidic protein solution and/or peptide composition derived therefrom can be applied alone or in admixture with conventional food or nutritive additives such as breading or batter coatings, spice dry rubs, cracker meal, corn meal or the like.
- the dry protein mixture, the dry alkaline protein mixture, the aqueous alkaline protein solution or aqueous acidic protein solution and/or peptide composition derived therefrom can be coated on the surface of the uncooked food with an applicator or can be coated by immersion tumbling the uncooked food in the solution or in a marinade containing the acidic aqueous protein solution, the dry alkaline protein mixture, or the aqueous alkaline protein solution or dry acidic protein mixture in a container or tumbling or vacuum tumbling apparatus.
- the dry protein mixture, dry alkaline protein mixture, aqueous acidic protein solution or aqueous alkaline protein solution also can contain flavorants such as butter flavor or garlic flavor or the like.
- dry protein mixture dry alkaline protein mixture, aqueous alkaline protein mixture or the aqueous acidic protein solution utilized in the present invention can be obtained by the following representative methods:
- reduce the pH of the aqueous alkaline solution to about 5.0-5.5 to precipitate the protein lower the pH of the precipitated protein to a pH of 4.0 or less to form a concentrated aqueous acidic protein solution and use the concentrated aqueous acidic solution or dry the solution and use the recovered dry protein.
- reduce the pH of the aqueous alkaline solution to about 5.0-5.5 to precipitate the protein lower the pH of the precipitated protein to a pH of 4.0 or less to form a concentrated aqueous acidic solution and use the concentrated aqueous acidic protein solution or dry the solution and use the recovered dry protein mixture.
- the protein products utilized in the present invention comprise primarily myofibrillar proteins that also contains significant amounts of sarcoplasmic proteins.
- the sarcoplasmic proteins in the protein product admixed with, injected into and/or coated on the uncooked food comprises above about 8%, preferably above about 10%, more preferably above about 15 % and most preferably above about 18%, up to about 30% by weight sarcoplasmic proteins, based on the total weight of protein in the dry protein mixture, dry alkaline protein mixture, the aqueous alkaline protein solution and/or aqueous acidic protein solution.
- the starting protein is derived from meat or fish, including shellfish muscle tissue.
- Representative suitable fish include deboned flounder, sole haddock, cod, sea bass, salmon, tuna, trout or the like.
- Representative suitable shellfish include shelled shrimp, crayfish, lobster, scallops, oysters or shrimp in the shell or like.
- Representative suitable meats include beef, lamb, pork, venison, veal, buffalo or the like; poultry such as chicken, mechanically deboned poultry meat, turkey, duck, a game bird or goose or the like.
- the dry protein mixture, dry alkaline protein mixture, aqueous alkaline protein solution or aqueous acidic protein solution of myofibrillar proteins and sarcoplasmic protein is mixed with one or more enzymes, which convert the protein to peptides thereby to produce a peptide composition which is added to food prior to cooking the food in order to retain moisture cooked food.
- the enzymes can be exoproteases and can be active to produce peptides at an acidic pH, an alkaline pH or a neutral pH.
- Representative suitable enzymes useful at acidic pH include Enzeco Fungal Acid Protease (Enzyme Development Corp., New York, NY; Newlase A (Amano, Troy, VA); and Milezyme 3.5 (Miles Laboratories, Elkhart, IN) or mixtures thereof.
- Representative suitable enzymes useful at alkaline pH include Alcalase 2.4 LFG (Novozyes, Denmark).
- Representative suitable enzymes useful at neutral pH include Neutrase 0.8L (Novozymes, Denmark) and papain (Penta, Livingston, NJ) or mixtures thereof. After, the peptides have been formed, their pH can be adjusted, either alone or in admixture with the protein composition of this invention to pH below about 4.0 or between about 10.5 and about 12.0 prior to applying them to an uncooked food to be cooked.
- the enzyme can be inactivated by changing pH of the protein composition with which it is mixed.
- the peptides formed by reaction of the protein composition with the enzyme composition then can be recovered by drying the solution wherein the reaction takes place. Drying can be effected by evaporation, spray drying, freeze-drying or the like.
- the peptides produced are instantaneously soluble in water at neutral pH.
- the peptide composition can be added to uncooked food for the purposes set forth above.
- the peptide products useful in this invention contain less than about 1 weight percent fats and oils (total), preferably less than about 0.2% weight percent fats and oils based on the weight of peptide.
- the peptide products utilized in the present invention contain less than about 2 weight percent ash, preferably less than about 0.2% weight percent fats and oils based on the weight of peptide. This low ash content is achieved by washing with water the protein starting material. Ash is defined as minerals, such as sodium, potassium, calcium, iron or phosphorous.
- the peptide products of this invention are instantly soluble in water to form a clear solution.
- the peptide products of this invention generally have lighter color whiteness units than the color whiteness units of a similar unhydrolyzed protein isolate from which they are derived as measured by a colorimeter with L, a, b capabilities.
- This lighter color is found with the hydrolyzed peptides of this invention derived from meats such as beef, pork or chicken as well as from dark muscle tissue from fish such as pelagic fish. This lighter color characteristic is desirable since it more easily permits dissolving the peptide product in water to form clear aqueous solutions.
- Color whiteness index is determined by converting the L, a, b values utilizing the formula: 100 [(100-L) 2 + a 2 + b 2 ] 05 . Color is measured using a tristimulus colorimeter utilizing the universally adopted "L, a, b" opponent-type scale developed by Richard Hunter as is well known in the art. "L” is a measure of light ranging from white to black. The “a” value measures the range from green to red, and the "b” value measures the range from blue to yellow. With these three coordinates, a three-dimensional value can be assigned to any color.
- the aqueous acidic protein solution, aqueous alkaline protein solution, the dry alkaline protein mixture or the dry protein mixture of myofibrillar proteins and sarcoplasmic proteins, and/or the peptide composition derived therefrom is applied to a surface of uncooked food to be cooked, or is injected into and/or is mixed with the uncooked food to be cooked.
- the uncooked food is both injected with and coated with the protein and/or peptide composition set forth above.
- the dry protein mixture, dry alkaline protein mixture, aqueous alkaline protein solution or aqueous acidic protein solution can be utilized alone or in admixture with a peptide composition derived therefrom. Alternatively, the peptide composition can be added alone to the uncooked food.
- a surface is a surface of uncooked food which is positioned 90 degrees from an adjacent surface or surfaces of the uncooked food.
- the term “a surface” can comprise the connecting surface connecting two adjacent surfaces positioned 90 degrees from each other.
- the entire surface of the uncooked food is coated with the dry acidic protein mixture, dry alkaline protein mixture, aqueous alkaline protein solution or aqueous acidic protein solution.
- the uncooked food containing the protein and/or the peptide then can be cooked at elevated temperature in acrylamide by the food being cooked.
- particulate food such as ground meat or fish, e.g. hamburger, or a food mixture such as a pastry for doughnuts is mixed with the dry protein mixture, dry alkaline protein mixture, aqueous alkaline protein solution or aqueous acidic protein solution comprising myofibrillar proteins and sarcoplasmic proteins and/or the peptide composition derived therefrom at a weight ratio usually comprising about 0.03 to about 18% weight of the protein mixture based on the weight of the uncooked food, preferably between about 0.5 and 10% weight based on the weight of uncooked food and most preferably comprising between about 0.5 to about 7% weight based on the weight of the uncooked food.
- the aqueous acidic protein solution, aqueous alkaline protein solution or peptide solution derived therefrom can be added to the food in the same ratios based on the weight of and/or peptide precooked food.
- the dry protein mixture, dry alkaline protein mixture, aqueous alkaline protein mixture or aqueous acidic protein solution and/ or peptide composition derived therefrom is applied to at least one surface of the food, the amount of the protein and/ or peptide mixture added is the same weight ratio as set forth above when mixed with uncooked food.
- the uncooked food can become undesirably hard.
- the uncooked food which is modified in accordance with this invention comprises vegetables, such as potato, corn, carrot or onion, tempura; nuts, mushrooms, flour based foods such as batter compositions, pastry compositions or the like. Additional foods include mushroom, nuts, batter compositions such as those comprising flour, egg and milk which can include additional food such as cornmeal, cracker meal or dusting meals.
- the food containing the dry protein mixture, dry alkaline protein mixture, aqueous alkaline protein solution or aqueous acidic protein solution and/or the peptide composition then can be cooked above about 14O 0 C in a conventional manner such as by deep fat frying, pan frying, baking or the like. It has been found that the cooked food provided in accordance with this invention contains between about 25% and about 95%, preferably between about 50% and about 95% less acrylamide by weight as compared to the same cooked food free of the protein and/or peptide composition of this invention.
- Example 1 Extracted chicken proteins to reduce acrylamide formation in deep fat fried potato.
- a chicken protein solution was manufactured according to US Patent No. 6,451 ,975 and concentrated using ultrafiltration and a 500,000 NWCO membrane filter (Koch Membrane, Wilmington, MA). Raw Russet potatoes suitable for french fries were obtained and cut into 3/8 inch strips and placed into cold water prior to frying.
- Frozen chicken breast pieces were ground (Stephan Micro-cut, Columbus, OH) and then acidified in phosphoric acid, pH 3.0 to form the chicken protein solution, 1.7 wt. % solution of dissolved solids. After ultrafiltration, a 3% Brix solution corresponding to an approximately 2.5wt/% protein solution was recovered.
- Sample 1 was a raw potato control which was not contacted with the protein solution.
- Sample 2 was a frozen raw potato control which was not contacted with the protein solution.
- Sample 3 was dipped into the chicken protein (3% Brix) and shaken to rid of excess protein (total approximately 5% pick-up), prior to being placed into a deep-fat fryer to fully cook for approximately 5 min, 30 seconds. Examples 1 and 2 were deep fat fried without any added protein. Product was analyzed for acrylamide content and the results are set forth in Table 1.
- the french fried potato made in accordance with this invention contain less than about 30% by weight acrylamide.
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- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Polymers & Plastics (AREA)
- Food Science & Technology (AREA)
- Nutrition Science (AREA)
- Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- General Preparation And Processing Of Foods (AREA)
- Meat, Egg Or Seafood Products (AREA)
- Preparation Of Fruits And Vegetables (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US73182105P | 2005-11-01 | 2005-11-01 | |
PCT/US2006/037007 WO2007053248A1 (en) | 2005-11-01 | 2006-09-25 | Process for reducing acrylamide in cooked food |
Publications (2)
Publication Number | Publication Date |
---|---|
EP1942751A1 true EP1942751A1 (de) | 2008-07-16 |
EP1942751A4 EP1942751A4 (de) | 2010-12-22 |
Family
ID=38006181
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
EP06804040A Withdrawn EP1942751A4 (de) | 2005-11-01 | 2006-09-25 | Verfahren zur reduktion von acrylamid in gegarten nahrungsmitteln |
Country Status (6)
Country | Link |
---|---|
EP (1) | EP1942751A4 (de) |
JP (1) | JP2009513134A (de) |
CN (1) | CN101299927A (de) |
AU (1) | AU2006309256A1 (de) |
CA (1) | CA2626010A1 (de) |
WO (1) | WO2007053248A1 (de) |
Families Citing this family (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2007046891A2 (en) | 2005-07-01 | 2007-04-26 | Mpf, Inc. | Systems and methods for separating proteins from connective tissue |
CN102805277A (zh) * | 2012-05-31 | 2012-12-05 | 中国农业大学 | 丙烯酰胺抑制剂及其应用 |
WO2019158866A1 (fr) | 2018-02-16 | 2019-08-22 | Saint-Gobain Glass France | Procede de depot d'un revetement intumescent organique sur feuille de verre |
WO2019158865A1 (fr) | 2018-02-16 | 2019-08-22 | Saint-Gobain Glass France | Vitrage anti-feu |
US20210307369A1 (en) * | 2020-04-03 | 2021-10-07 | Pacific Foods Solutions, LLC | Reducing fat absorption in prepared foods |
FR3119844A1 (fr) | 2021-02-16 | 2022-08-19 | Saint-Gobain Glass France | Vitrage anti-feu comprenant une feuille de verre revêtue d’un revêtement intumescent |
Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0848911A2 (de) * | 1996-12-21 | 1998-06-24 | Advanced Protein Technologies, Inc. | Verfahren zur Isolierung einer Proteinzusammensetzung aus einem Muskelsubstrat und Proteinzusammensetzung |
WO2004075657A2 (en) * | 2003-02-21 | 2004-09-10 | Frito-Lay North America, Inc. | Method for reducing acrylamide formation in thermally processed foods |
WO2004089111A1 (de) * | 2003-04-11 | 2004-10-21 | Basf Aktiengesellschaft | Verfahren zur verminderung der acrylamidbildung beim erhitzen von aminogruppenhaltigen verbindungen |
US20050069626A1 (en) * | 2002-09-24 | 2005-03-31 | Kelleher Stephen D. | Food product and process for reducing oil and fat content in cooked food |
WO2005077203A2 (en) * | 2004-02-09 | 2005-08-25 | Cargill, Incorporated | Low acrylamide food |
EP1568283A1 (de) * | 2002-11-27 | 2005-08-31 | Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo | Verfahren zur hemmung der acrylamidbildungund seine verwendung |
US20050214411A1 (en) * | 2004-03-29 | 2005-09-29 | Lindsay Robert C | Methods for suppressing acrylamide formation and restoring browned color and flavor |
Family Cites Families (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6451975B1 (en) * | 1996-12-21 | 2002-09-17 | Advanced Protein Technologies, Inc. | Protein composition and process for isolating a protein composition from a muscle source |
US7393550B2 (en) * | 2003-02-21 | 2008-07-01 | Frito-Lay North America, Inv. | Method for reducing acrylamide formation in thermally processed foods |
KR100525178B1 (ko) * | 2003-03-12 | 2005-11-01 | 주식회사농심 | 아크릴아마이드 저감화 스낵 및 이의 제조방법 |
JP2004313183A (ja) * | 2003-04-04 | 2004-11-11 | House Foods Corp | 食品中のアクリルアミドの低減方法 |
US20050048172A1 (en) * | 2003-09-02 | 2005-03-03 | Vattem Dhiraj A. | Compositions of legume proteins and methods of use thereof for reducing acrylamide in cooked foods |
-
2006
- 2006-09-25 EP EP06804040A patent/EP1942751A4/de not_active Withdrawn
- 2006-09-25 JP JP2008537712A patent/JP2009513134A/ja active Pending
- 2006-09-25 WO PCT/US2006/037007 patent/WO2007053248A1/en active Application Filing
- 2006-09-25 CA CA002626010A patent/CA2626010A1/en not_active Abandoned
- 2006-09-25 CN CNA2006800406428A patent/CN101299927A/zh active Pending
- 2006-09-25 AU AU2006309256A patent/AU2006309256A1/en not_active Abandoned
Patent Citations (7)
Publication number | Priority date | Publication date | Assignee | Title |
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Also Published As
Publication number | Publication date |
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EP1942751A4 (de) | 2010-12-22 |
CA2626010A1 (en) | 2007-05-10 |
CN101299927A (zh) | 2008-11-05 |
JP2009513134A (ja) | 2009-04-02 |
WO2007053248A1 (en) | 2007-05-10 |
AU2006309256A1 (en) | 2007-05-10 |
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