Classifications

• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23B—PRESERVATION OF FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES; CHEMICAL RIPENING OF FRUIT OR VEGETABLES
  • A23B4/00—Preservation of meat, sausages, fish or fish products
  • A23B4/14—Preserving with chemicals not covered by groups A23B4/02 or A23B4/12
  • A23B4/18—Preserving with chemicals not covered by groups A23B4/02 or A23B4/12 in the form of liquids or solids
  • A23B4/20—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 OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • 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
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • 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
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
  • A23L13/50—Poultry products, e.g. poultry sausages
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
  • A23L13/60—Comminuted or emulsified meat products, e.g. sausages; Reformed meat from comminuted meat product
• • A—HUMAN NECESSITIES
  • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
  • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
  • A23L17/00—Food-from-the-sea products; Fish products; Fish meal; Fish-egg substitutes; Preparation or treatment thereof

Definitions

• This invention relates to a process for retaining liquid in cooked food. More particularly, this invention relates to such a process which utilizes a peptide composition derived from animal muscle protein to retain moisture in food and to the food product utilized in the process.
• meat or fish cooked at an elevated temperature loses its moisture to the surrounding atmosphere. In so doing, the cooked meat or fish undesirably loses its natural or added flavors so that it becomes less tasteful. Fluid loss during cooking of meat or fish can range up to 30% to 40% by weight based upon the weight of the meat or fish prior to cooking.
• a prior solution for retaining moisture in the meat or fish without additives took the form of wrapping the meat or fish in a solid moisture barrier such as aluminum foil. This solution is undesirable since the surface of the meat or fish remains soft rather than having a desirable crust.
• Prior attempts to retain moisture in cooked meat or fish with additives have included the use of sodium tripolyphosphate, a coating of fat free flour, based, batter containing an egg white substitute (U.K. Patent Application 2,097,646), water-in-oil emulsion (U.S. Pat. No. 3,406,081), protein or protein isolate and a fat (U.S. Pat. Nos. 4,031 ,261 and 4,935,251), milk solids (U.S. Pat. No. 2,282,801) and lecithin (U.S. Pat. Nos. 2,470,281 and 3,451,826).
• animal muscle tissue or vegetable to be cooked is coated or admixed or injected with a dry peptide mixture or an aqueous acidic peptide solution each derived from a protein composition which, in turn, is derived from a mixture of myofibrillar proteins and sarcoplasmic proteins.
• the mixture of myofibrillar proteins and sarcoplasmic protein is derived from animal muscle tissue.
• the protein composition derived from animal muscle tissue is obtained by one of the processes disclosed in U.S. Pat. Nos. 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 peptide mixture as used herein is meant a dehydrated, peptide mixture derived from a mixture of myofibrillar proteins and sarcoplasmic proteins which, in turn, is derived from animal muscle tissue and which is obtained from an aqueous acid solution (less than or equal to pH 4.5) or an aqueous alkaline solution (greater than or equal to pH 10.5) and having a final pH of about 4.5 or less or between pH 6.5 and 8.5.
• the dry peptide 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 peptide mixture and water.
• Peptides directly derived from solutions having a pH of 8.5 or above are less preferred in the present invention.
• the acidic peptide compositions are preferred for use in the present invention, particularly those having a pH of 3.5 or less, and most preferably a pH between about 2.5 and about 3.5.
• aqueous acidic peptide solution an aqueous solution of peptides derived from a mixture of myofibrillar proteins and sarcoplasmic proteins, which in turn, is derived from animal muscle tissue and having a pH of 4.5 or less, preferably 3.5 or less and most preferably between about 2.5 and about 3.5 but not so low as to adversely affect the peptide functionality.
• the aqueous acidic peptide solution can be obtained directly from animal muscle tissue acidic protein solution by the processes described below or by dissolving the dry peptide mixture in water or in a pharmaceutically or food grade acceptable aqueous acidic solution.
• the peptide composition of this invention to retain moisture in cooked foods can be utilized alone or in admixture with the mixture of myofibrillar proteins and saracoplasmic proteins derived from animal muscle tissue described herein.
• the fish, meat or vegetable containing the dry peptide mixture or aqueous acidic peptide solution then can be cooked at elevated temperature in the absence of a solid moisture barrier while retaining a substantial majority of its original moisture.
• the difference in weight between meat, fish or vegetable treated in accordance with this invention compared with fish, meat or vegetable not injected, mixed or coated with the dry peptide mixture or aqueous acidic peptide solution is between about 4 and about 21%, more usually, between about 4 and about 10%.
• 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 3.5 or less, 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 resultant aqueous acidic peptide solution can be dried such as by spray drying or lyophilization or evaporation to form a peptide powder.
• the peptide powder or aqueous acidic peptide solution then is added to the meat, fish or vegetable.
• the resultant meat, fish or vegetable containing the peptide composition retains a substantial portion of its moisture during cooking.
• 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.
• 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 protein-rich layer 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 pH of the protein-rich aqueous phase can be lowered to a pH about 3.5 or below, preferably between about 2.5 and 3.5.
• the protein in the aqueous acidic solution is recovered after centrifugation (when used) or 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 pH of the precipitated protein then is raised to between 6.5 and 8.5 and a solid product is recovered such as by drying including spray drying, lyophilization or evaporation or which can be comminuted and converted to the peptide composition with an enzyme.
• the peptide composition described above then is added to the uncooked fish, meat, poultry or vegetable.
• the precipitated protein can be mixed with a pharmaceutically acceptable or food grade acid to form an aqueous acidic protein solution of a desired viscosity.
• the latter process is particularly suitable for forming an aqueous acidic protein solution that can be converted to a peptide solution with an enzyme and then injected into the uncooked food.
• the peptide composition derived from the dry protein mixture or the aqueous acidic protein solution is applied to, admixed with and/or injected into the uncooked food.
• the peptide composition 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. It is preferred to utilize the aqueous acidic peptide solution, with or without food or nutritional additives, for injection.
• the dry peptide mixture and /or aqueous peptide solution can be coated on the surface of the uncooked meat, fish or vegetable with an applicator or can be coated by tumbling or immersing the uncooked meat, fish or vegetable in the solution or in a marinade containing the acidic aqueous peptide solution or dry acidic protein mixture in a container or in a tumbling or vacuum tumbling apparatus.
• aqueous basic solution reduces the pH of the aqueous basic solution to about 5.0-5.5 to precipitate the protein, lower the pH of the precipitated protein to a pH of 4.5 or less to form a concentrated aqueous acidic solution and use the concentrated aqueous acidic solution or dry the solution and use the recovered dry protein.
• reduce the pH of the aqueous basic solution to about 5.0-5.5 to precipitate the protein raise the pH of the precipitated protein to 6.5-8.5, dry and comminute the protein.
• reduce the pH of the aqueous basic solution to about 5.0-5.5 to precipitate the protein raise the pH of the precipitated protein to 6.5-8.5, dry and comminute the protein.
• aqueous basic solution reduces the pH of the aqueous basic solution to about 5.0-5.5 to precipitate the protein, lower the pH of the precipitated protein to a pH of 4.5 or less to form a concentrated aqueous acidic solution and use the concentrated aqueous acidic solution or dry the solution and use the recovered dry protein.
• a peptide composition derived from the protein mixture having a pH between about 2.5 and 3.5 It is preferred to utilize a peptide composition derived from the protein mixture having a pH between about 2.5 and 3.5.
• the peptide composition can be utilized alone or can be mixed with a protein composition derived from animal muscle tissue described above and then added to the uncooked food for the purpose of retaining moisture in cooked food.
• the starting protein is derived from meat or fish, including shellfish.
• 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 peptides formed by reaction of the protein composition with the enzyme composition then are 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 by the present invention are instantaneously soluble in. water at neutral pH.
• the peptide products utilized in the invention typically 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 typically 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 can be 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 calorimeter 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 as shown, for example, in Example 1 below.
• 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 ] ° 5 . Color is measured using a tristimulus calorimeter 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 protein products utilized to form the peptide composition utilized in the present invention comprise primarily myofibrillar proteins that also contains significant amounts of sarcoplasmic proteins.
• the sarcoplasmic proteins in the protein product utilized to form the peptide composition added to fish, meat, poultry or vegetable 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 acidic protein mixture or aqueous acidic protein solution.
• the dry peptide mixture derived from a mixture of myofibrillar proteins and sarcoplasmic proteins, in powder form, small coarse particle or dehydrated form is applied to the surface of animal muscle tissue or vegetable to be cooked, or is mixed with the animal muscle or vegetable tissue to be cooked such as hamburger, sliced reformulated beef or sausage.
• a surface as used herein is a surface of the fish or meat which is positioned 90 degrees from an adjacent surface or surfaces of the meat or fish.
• the term "a surface” can comprise the connecting surface connecting two adjacent surfaces positioned 90 degrees from each other.
• the entire surface of the meat, fish, poultry or vegetable is coated with the dry acidic protein mixture or aqueous acidic protein solution. The coated fish, meat, poultry or vegetable then can be cooked at elevated temperature while retaining a substantial majority of its original moisture.
• particulate meat or fish such as ground meat or fish, e.g. hamburger
• the dry peptide mixture derived from a protein mixture comprising myofibrillar proteins and sarcoplasmic proteins at a weight ratio usually comprising about 0.03 to about 18% weight of the protein mixture based on the weight of the uncooked meat, fish or vegetable, preferably between about 0.5 and 10% weight based on the weight of uncooked meat, fish, poultry or vegetable and most preferably comprising between about 0.5 to about 5% weight based on the weight of the uncooked food.
• the aqueous acidic peptide solution can be added to the meat, fish, poultry or vegetable in the same ratios based on the weight of peptide in the solution.
• the dry peptide mixture or aqueous acidic peptide can be added as a mixture with the protein composition described above at the same weight % based on the weight of uncooked food.
• the amount of the peptide mixture added is the same weight ratio as set forth above when mixed with ground meat or fish.
• the cooked meat, fish or vegetable can become undesirably hard.
• the animal muscle tissue which is modified in accordance with this invention comprises meat, poultry or fish, including shell fish.
• Representative suitable fish include deboned flounder, sole, haddock, cod, sea bass, salmon, tuna, trout or the like.
• Representative suitable shell fish include shelled shrimp, crabmeat, crayfish, lobster, scallops, oysters, or shrimp in the shell or the like.
• Representative suitable meats include ham, 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 either in fillet form or in ground form such as hamburg.
• Representative suitable vegetables include potato and onion.
• the meats can include the bone of the animal when the bone does not adversely affect the edibility of the meat such as spare ribs, lamb chops or pork chops.
• processed meat products which include animal muscle tissue such as a sausage composition, a hot dog composition, emulsified product or the like can be coated, injected or mixed with the dry acidic peptide mixture and/or the aqueous acidic peptide solution, or a combination of these peptide addition methods.
• Sausage and hot dog compositions include ground meat or fish, herbs such as sage, spices, sugar, pepper, salt and fillers such as dairy products as is well known in the art.
• the fish, meat, poultry or vegetable containing the dry peptide mixture or aqueous acidic peptide solution either alone or in admixture with the protein composition described above then can be cooked in a conventional manner such as by baking, broiling, deep fat frying, pan frying, in a microwave oven or the like. It has been found that the cooked meat, fish or vegetable provided in accordance with this invention weighs between about 4% and about 21%, more usually between about 4% and about 9% by weight greater than cooked untreated meat, fish or vegetable starting from the same uncooked weight.
• Percent (%) in Tables 1-8 reflects the comparative loss of moisture in the controls verses the moisture loss in the compositions of this invention (moisture content of a composition of this invention/moisture content of control X 100).
• Chicken protein isolate from myofibrillar and sarcoplasmic proteins was produced according to U.S. Pat. No. 6,005,073 (low pH) from chicken breast muscle; and freeze-dried until it contained approximately 5% moisture.
• the aqueous acidic protein solution from which the dry protein mixture was obtained had a pH of 2.68.
• the dry protein mixture (protein isolate) was incorporated into fresh, ground beef (75% lean) by hand kneading for 1 min and shaped into hamburgers of uniform size. To approximately one-quarter Ib. of beef (exactly weighed) was added 0-1.5 grams of the dried protein isolate.
• the hamburgers were pan-fried on an Iwatani (Tokyo, Japan) portable butane grill on high temperature for a total of 15 min (10 min then flipped and additional 5 min).
• the internal centers of the hamburgers reached 150 ° F. ⁇ 2° F. after cooking.
• the cooked hamburgers were drained on paper towels for twenty seconds prior to weighing (two decimal places).
• Example 2 Incorporation (Cod Protein Isolate-Acid) Cod protein isolate from myofibrillar and sarcoplasmic proteins was produced according to U.S. Pat. No. 6,005,073 (low pH) from fresh Atlantic cod muscle. The aqueous acidic protein solution recovered was adjusted to pH 5.5 to enact protein precipitation. The pH of the precipitate was then raised to pH 7.04 and freeze-dried until it contained approximately 7% moisture.
• the dry protein mixture (protein isolate) was incorporated into fresh, ground beef (75% lean) by hand kneading for 1 min and shaped into hamburgers of uniform size. To approximately one-quarter Ib. of beef (exactly weighed) was added 0-1.5 grams of dried protein isolate. The hamburgers were pan-fried on an Iwatani (Tokyo, Japan) portable butane grill on high temperature for a total of 15 min (10 min then flipped and additional 5 min). The internal centers of the hamburgers reached 155 ° F ⁇ 2 0 F after cooking. The cooked hamburgers were drained on paper towels for twenty seconds prior to weighing (two decimal places).
• Chicken protein isolate from myofibrillar and sarcoplasmic proteins was produced according to U.S. Pat. No. 6,136,959 (high pH) from chicken breast muscle.
• a dry protein isolate was obtained by precipitation at a pH of 5.5 followed by a readjustment of the precipitate pH to pH 7.12 and subsequently freeze dried.
• the dry protein mixture (protein isolate) was incorporated into fresh, ground beef (80% lean) by hand kneading for 1 min and shaped into hamburgers of uniform size.
• To beef (exactly weighed) was added 0 and 4.0 grams of dried protein isolate.
• the hamburgers were cooked on high in a Sharp Carousel (1000 watt) microwave oven for a total of 1 10 seconds (no flipping).
• the internal centers of the hamburgers reached 183 ° F ⁇ 4° F after cooking.
• the cooked hamburgers were drained on paper towels for twenty seconds prior to weighing (two decimal places).
• Example 4 Incorporation (Chicken Protein Isolate- Acid— Adjusted to pH 5.5) Chicken protein isolate from myofibrillar and sarcoplasmic proteins was produced according to U.S. Pat. No. 6,005,073 (low pH) from fresh chicken muscle and readjusted to pH 5.5. Moisture content of the precipitate was 74%.
• the protein isolate was chopped in a Waring food processor for 20 seconds to reduce size and was incorporated into fresh, ground chicken breast by hand kneading for 1 min prior to being shaped into patties of uniform size.
• the chicken pieces were cooked on high in ZipLock.RTM. disposable containers in a Sharp Carousel (1000 watt) microwave oven for 20 seconds, flipped and microwaved an additional 20 seconds. The internal centers of the chicken pieces reached 190.° F ⁇ 0 ° F. after cooking. The cooked chicken pieces were drained on paper plates prior to weighing (two decimal places).
• Chicken protein isolate from myofibrillar and sarcoplasmic proteins was produced according to U.S. Pat. No. 6,005,073 (low pH) from chicken breast muscle.
• a dry protein isolate was obtained by precipitation at a pH of 5.5 followed by a readjustment of the precipitates to pH 6.73 and subsequently was freeze-dried until it contained approximately 5% moisture.
• Fresh chicken breasts were cut into uniform portions, weighed and pressed into a dish containing the dry protein mixture (protein isolate) until coated (with varying amounts of coating).
• the coated chicken pieces were cooked on high in ZipLock.RTM. disposable containers in a Sharp Carousel (1000 watt) microwave oven for 20 seconds, flipped and microwaved an additional 20 seconds.
• the internal centers of the chicken pieces reached 179 ° F ⁇ 0 ° except for the control, which reached 172 0 F. after cooking.
• the cooked chicken pieces were drained on paper plates prior to weighing (two decimal places).
• the chicken pieces containing between 0.97-1.75 g protein isolate had improved color, were shiny in appearance on the chicken's interior, and had much greater juiciness and better mouth-feel than the control. (0.00 g. Protein isolate).
• the coated pieces retained their original size and shape, whereas the control was very shape distorted. A large pool of moisture was found in the control container and very little to none in the coated pieces containers.
• the chicken piece coated on one-side only had slight distortion in size and a small amount of pooled moisture was found in the container after cooking.
• Dry acidic protein mixtures from chicken breast, Atlantic cod fillet, and pork loin containing myofibrillar and sarcoplasmic proteins were produced according to U.S. Pat. No. 6,005,073 (low pH). Dry protein isolates were obtained by precipitation at pH'sabout 5.5 followed by readjustment of the precipitate's pH to about neutrality. The precipitates subsequently were freeze-dried. Atlantic cod isolate was manufactured using 0.1% (of the total water weight) sodium tripolyphosphate prior to homogenization as a metal chelating antioxidant. Pieces to be coated were cut into uniform portions, weighed and pressed into a dish containing the dried protein isolates until coated (with varying amounts of coating). The coated chicken pieces were cooked on high in ZipLock.RTM. disposable containers in a Sharp Carousel (1000 watt) microwave oven at 20 second intervals until an internal temperature in the centers of the muscle pieces reached 172. °. F. The cooked pieces were drained on paper plates prior to weighing (two decimal places).
• the pieces containing protein isolate were shiny in appearance on the interior and had much greater juiciness and better mouth-feel than the controls (0.00 g. Protein isolate).
• the coated pieces retained their original size and shape, whereas the controls were very shape distorted. Large pools of moisture were found in the controls containers and very little to none in the coated pieces containers.
• Example: 7 Coating (Chicken Protein Isolate- Acid— Adjusted to pH 5.5) Protein isolate from chicken breast myofibrillar and sarcoplasmic proteins was produced according to U.S. Pat. No. 6,005,073 (low pH) and readjusted to pH 5.5. Moisture content of the precipitate was 74%. One sample was freeze-dried at pH 5.5 until a moisture content of approximately 6%. Pieces to be coated were cut into uniform portions, weighed and pressed into a dish containing the pH 5.5 protein isolates until coated (with varying amounts of coating). The coated chicken pieces were cooked on high in ZipLock.RTM.
• Example 4 illustrates that a substantially neutral pH form of the protein composition is not useful in the present invention.
• Example 8 Inject into Chicken (Chicken Protein Isolate pH 2.8 Acid)
• Protein isolate from chicken breast myofibrillar and sarcoplasmic proteins was produced according to U.S. Pat. No. 6,005,073 (low pH). The protein precipitate obtained at pH 5.5 was readjusted back to pH 2.8 using 2 M HCl. The thick consistency solution thus produced contained 3.7% protein.
• Chicken breast pieces to be coated were cut into uniform portions, weighed and injected using a BD 5 ml syringe (25 gauge needle) with different amounts of weighed protein (pH 2.8) solution. The injected chicken pieces were cooked on high in ZipLock.RTM. disposable containers in a Sharp Carousel (1000 watt) microwave oven at 20 second intervals until an internal temperature in the centers of the chicken pieces reached 170 ° F ⁇ 7 ° F. The cooked chicken pieces were drained on paper plates prior to weighing (two decimal places).
• Example 9 Inject into Chicken (Pork Protein Isolate pH 2.8 Acid)
• Protein isolate from pork loin myofibrillar and sarcoplasmic proteins was produced according to U.S. Pat. No. 6,005,073 (low pH). The precipitate at pH 5.5 was readjusted back to pH 2.8 using 2 M HCl and 0.5% NaCl (w/w). The solution was found to be 2.25% protein.
• Chicken breast pieces to be coated were cut into uniform portions, weighed and injected using a BD 5 ml syringe (18 gauge needle) with protein (pH 2.8) solution. The injected chicken pieces were cooked on high in ZipLock.RTM. disposable containers in a Sharp Carousel (1000 watt) microwave oven at 20 second intervals for a total of 80 seconds. The internal temperature in the centers of the chicken pieces reached 176° F for the control and 198 0 F for the treated sample. The cooked chicken pieces were drained on paper plates prior to weighing (two decimal places).
• the piece containing protein isolate was shiny in appearance and had much greater juiciness and better mouth-feel than the control.
• the injected piece retained its original size and shape. A large pool of moisture was found in the control container and very little to none in the injected piece container.
• Example 10 Fish Protein Isolate-Acid Fish protein isolate from myofibrillar and sarcoplasmic proteins was produced according to U.S. Pat. No. 6,451 ,975 (low pH, no centrifugation) from fresh haddock.
• the aqueous protein solution was made using citric acid (0.9%) and food-grade, hydrochloric acid 2N (for fine pH adjustment) resulting in final pH of 3.50, salt 2.04 mS, and 6.0% Brix.
• Haddock pieces were cut into somewhat uniform portions, weighed and injected using a BD 10 ml syringe (25 gauge needle) with different amounts of weighed protein (pH 3.50) solution. The injected haddock pieces were cooked on high in ZipLock.RTM.
• the injected pieces retained a great deal of their original size and shape, whereas the control shrunk to a greater extent and had a larger pool of moisture remaining in the cooking container. Two of the samples had higher end weights than their original muscle weights after cooking.
• Example 11 Coating using Hydrolyzed Proteins to Retain Moisture
• a hake protein solution was manufactured according to U.S. Pat. No. 6,451,975 and concentrated using ultrafiltration and a 500,000 NWCO membrane (Koch Membrane, Wilmington, Mass.). Hake muscle tissue was minced and mixed with phosphoric acid and ultrafiltered to form a 3.2% BRIX solution. This solution is diluted with water to form a 2.5% BRIX solution having a viscosity of 11 seconds at 36° F. using a Zahn #5 cup. The hake protein solution was incubated with proteolytic enzymes for 60 min. at 9.9° C. in beakers. The enzyme concentrations were at 0.1% (w/w).
• Papain (Acros Organics, Geel, Belgium) was added to the hake protein solution adjusted to pH 7.04 using 2N NaOH, and Pepsin (Fisher Chemical, Fair Lawn, NJ.) was added to the protein solution, adjusted to pH 3.06.
• a substantial breakdown in viscosity of the enzyme treated protein solutions occurred during the incubation period, especially with the papain samples.
• Zahn viscometers viscosity readings, measured in Zahn seconds, were reduced by 67% in papain, and 16% in the pepsin treated samples.
• the hydrolyzed protein solutions were subsequently used as described below as dips for pollock.
• Wedges (0.75 oz) were cut from frozen Pollock blocks and sequenced through a batter/predust/batter/bread routine using a crunchy coating system (Newly Wed Foods, Chicago, 111.).
• the breaded portions (1.5 oz.) were dipped into the hydrolyzed protein solutions for approximately 1 sec and drained prior to being refrozen.
• the dipped frozen portions were fried on-line for 23 sec. at 375° F. using hydrogenated, soybean oil, refrozen and analyzed.

Landscapes

• Life Sciences & Earth Sciences (AREA)
• Chemical & Material Sciences (AREA)
• Engineering & Computer Science (AREA)
• Health & Medical Sciences (AREA)
• Food Science & Technology (AREA)
• Polymers & Plastics (AREA)
• Nutrition Science (AREA)
• Zoology (AREA)
• Microbiology (AREA)
• Marine Sciences & Fisheries (AREA)
• Molecular Biology (AREA)
• Mycology (AREA)
• Chemical Kinetics & Catalysis (AREA)
• General Chemical & Material Sciences (AREA)
• Wood Science & Technology (AREA)
• Meat, Egg Or Seafood Products (AREA)
• Peptides Or Proteins (AREA)

Priority Applications (5)

Applications Claiming Priority (2)

Publications (2)

Family

ID=36319595

Family Applications (1)

Country Status (9)

Families Citing this family (15)

Family Cites Families (11)

• 2004
  • 2004-10-29 US US10/976,433 patent/US7160567B2/en not_active Expired - Lifetime
• 2005
  • 2005-09-27 EP EP05800119A patent/EP1806984A4/en not_active Withdrawn
  • 2005-09-27 WO PCT/US2005/034766 patent/WO2006049756A2/en not_active Ceased
  • 2005-09-27 MX MX2007005135A patent/MX2007005135A/es not_active Application Discontinuation
  • 2005-09-27 CA CA002583109A patent/CA2583109A1/en not_active Abandoned
  • 2005-09-27 RU RU2007119423/13A patent/RU2370102C2/ru not_active IP Right Cessation
  • 2005-09-27 AU AU2005301229A patent/AU2005301229A1/en not_active Abandoned
  • 2005-09-27 JP JP2007538934A patent/JP2008517624A/ja active Pending
  • 2005-09-27 CN CNA2005800371227A patent/CN101048082A/zh active Pending

Also Published As

Similar Documents

Legal Events