WO2019221752A1 - Inhibition de la gélification du jaune d'œuf au cours de la congélation - Google Patents

Inhibition de la gélification du jaune d'œuf au cours de la congélation Download PDF

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Publication number
WO2019221752A1
WO2019221752A1 PCT/US2018/033473 US2018033473W WO2019221752A1 WO 2019221752 A1 WO2019221752 A1 WO 2019221752A1 US 2018033473 W US2018033473 W US 2018033473W WO 2019221752 A1 WO2019221752 A1 WO 2019221752A1
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Prior art keywords
yolk
egg yolk
gelation
hydrolyzed
egg
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PCT/US2018/033473
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English (en)
Inventor
Tong Wang
Nuria ACEVEDO
Monica PRIMACELLA
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Iowa State University Research Foundation, Inc.
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Priority to PCT/US2018/033473 priority Critical patent/WO2019221752A1/fr
Publication of WO2019221752A1 publication Critical patent/WO2019221752A1/fr

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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
    • A23L15/00—Egg products; Preparation or treatment thereof
    • 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
    • A23B5/00—Preservation of eggs or egg products
    • A23B5/04—Freezing; Subsequent thawing; Cooling
    • A23B5/041—Freezing or cooling without shell
    • 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
    • A23B5/00—Preservation of eggs or egg products
    • A23B5/04—Freezing; Subsequent thawing; Cooling
    • A23B5/05—Freezing or cooling with addition of chemicals
    • A23B5/055—Freezing or cooling with addition of chemicals with direct contact between the food and the chemical, e.g. liquid nitrogen, at cryogenic temperature

Definitions

  • the present invention relates to food additives that affect egg yolk gelation induced by freezing.
  • Egg yolk in its fluid form, is a valuable food ingredient for the manufacture of many food products.
  • a large quantity of liquid yolk is frozen commercially for prolonged storage of up to one year (Au et al,“Determination of the Gelation Mechanism of Freeze- Thawed Hen Egg Yolk,” Journal of Agricultural andFood Chemistry 63(46): 10170-10180 (2015)).
  • the benefits of storing egg yolk in the frozen state are prevention of microbial growth and spoilage, retention of egg yolk flavor and color, and inhibition of chemical reactions such as autoxidation of lipids and the browning reaction (Powrie,“Gelation of Egg Yolk upon Freezing and Thawing,” In Low Temperature Biology of Foodstuffs: Recent Advances in Food Science 4:319-331 (1968)).
  • autoxidation of lipids and the browning reaction Powrie,“Gelation of Egg Yolk upon Freezing and Thawing,” In Low Temperature Biology of Foodstuffs: Recent Advances in Food Science 4:319-331 (1968)
  • an irreversible alteration in fluidity known as gelation occurs (Moran,“The Effect of Low Temperature on Hens' Eggs,” Proceedings of the Royal Society of London. Series B, Containing Papers of a Biological Character 98(691):436-456 (1925)).
  • This physiological change is undesirable because of reduced yolk dispersibility in water and loss of functionality.
  • LDL low-density lipoproteins
  • HDL high-density lipoproteins
  • the present invention is directed to overcoming these and other deficiencies in the art.
  • One aspect of the invention relates to a method for inhibiting egg yolk gelation resulting from freezing and thawing
  • This method comprises treating egg yolk with an effective amount of a compound selected from the group consisting of amino acids, hydrolyzed proteins, hydrolyzed carboxymethyl cellulose, polyethylene glycol, and sorbitan esters, to improve the gelation properties of egg yolk.
  • Another aspect of the invention relates to an egg yolk-containing product having inhibited susceptibility to gelation resulting from freezing further comprising the compound selected from the group consisting of amino acids, hydrolyzed proteins, hydrolyzed
  • carboxymethyl cellulose carboxymethyl cellulose, polyethylene glycol, and sorbitan esters.
  • hydrophobicity, and lipoprotein particle size before and after freezing were evaluated and compared.
  • Figures 1A-1D are graphs showing the effect of rotor-stator mixing speed
  • Figures 2A-2B are graphs showing the effect of various additives (Figure 2A) and quantity of additives (Figure 2B) on hardness of frozen-thawed yolk (stored at -20°C for 45 hours). Values with different letters are significantly different (p ⁇ 0.05).
  • Figures 3A-3B are graphs showing the hardness of frozen-thawed yolk treated with HCMC of different molecular weights, and frozen at -20°C for 5 days ( Figure 3 A) and 1 day at 2% (w/w) concentration ( Figure 3B). Values with different letters are significantly different (p ⁇ 0.05).
  • Figures 4A-4G are graphs showing the hardness of frozen-thawed yolk (stored at -
  • Figures 5A-5C are graphs showing the effect of colloid milling and additives on hardness (Figure 5A) and particle size distribution ( Figures 5B and 5C) of yolk frozen at -20°C for 45 hours.
  • Abbreviations are F, fresh; G, frozen-thawed; CM, colloid milled.
  • Figure 6 shows schematic illustrations of the proposed gelation-inhibiting mechanism by FICMC, proline, and peptide in frozen-thawed egg yolk.
  • Figures 7A-7C are graphs showing the particle size distribution (Figure 7A), protein surface hydrophobicity (Figure 7B), and amount of freezable water (Figure 7C) of yolk containing various additives.
  • Abbreviations are F, fresh yolk; G, frozen-thawed yolk (stored at - 20°C for 45 hours).
  • One aspect of the invention relates to a method for inhibiting egg yolk gelation resulting from freezing and thawing.
  • This method comprises treating egg yolk with an effective amount of a compound selected from the group consisting of amino acids, hydrolyzed proteins, hydrolyzed carboxymethyl cellulose, polyethylene glycol, and sorbitan esters, to improve the gelation properties of egg yolk.
  • whole egg means a mixture of egg white and yolk.
  • the whole egg may, but does not necessarily, include egg white and egg yolk in a ratio recognized as the ratio of yolk to white in eggshells.
  • Whole egg products can include other optional ingredients as described below.
  • the term "egg yolk” means egg yolk obtained after separating the white and the yolk by breaking fresh eggs, and as such, the egg yolk is substantially free of egg white.
  • the egg yolk can be used in the disclosed products that can comprise other optional ingredients as described below.
  • the term "egg white” means egg white obtained after separating the white and the yolk by breaking fresh eggs, and as such, the egg white is substantially free of egg yolk.
  • the egg white can be used in the disclosed products that can comprise other optional ingredients as described below.
  • Amino acids that can be used according to the present invention can be any natural or non-natural amino acid, including alpha amino acids, beta amino acids, gamma amino acids, L-amino acids, and D-amino acids.
  • Suitable amino acids that can be used according to the present invention include, but are not limited to, histidine (His), isoleucine (He), leucine (Leu), lysine (Lys), methionine (Met), phenylalanine (Phe), threonine (Thr), tryptophan (Trp), valine (Val), arginine (Arg), cysteine (Cys), glutamine (Gin), glycine (Gly), proline (Pro), serine (Ser), tyrosine (Tyr), alanine (Ala), asparagine (Asn), aspartic acid (Asp), glutamic acid (Glu), and selenocysteine (Sec).
  • hydrolyzed proteins or“protein hydrolysates” refers to proteins that have been hydrolyzed or broken down into shorter peptide fragments and amino acids.
  • Suitable protein sources for hydrolyzed proteins include milk, soy, rice, meat
  • Suitable proteins include, but are not limited to, soy based, milk based, casein protein, whey protein, rice protein, beef collagen, pea protein, potato protein and mixtures thereof.
  • Suitable protein hydrolysates also include, but are not limited to, soy protein hydrolysate, casein protein hydrolysate, whey protein hydrolysate, rice protein hydrolysate, potato protein hydrolysate, fish protein hydrolysate, egg hydrolysate, gelatin protein hydrolysate, a combination of animal and vegetable protein hydrolysates, and mixtures thereof.
  • the term“hydrolyzed egg white protein” or“hydrolyzed egg white” refers to a product of a hydrolysis of egg white protein. Wherein the product can be fully or partially hydrolyzed. Wherein the product is chemically or enzymatically hydrolyzed.
  • the term“hydrolyzed egg yolk protein” or“hydrolyzed egg yolk” refers to a product of a hydrolysis of yolk white protein. Wherein the product can be fully or partially hydrolyzed. Wherein the product is chemically or enzymatically hydrolyzed.
  • Hydrolyzed egg yolk protein and hydrolyzed egg white protein are short-chain peptides produced by enzymatic hydrolysis of egg white or egg yolk, wherein the short-chain peptides have MW no larger than l5kDa.
  • the compound is short-chain peptides produced by enzymatic hydrolysis of egg white or egg yolk.
  • This short-chain peptide has MW between O. lkDa and l5kDa, between 0.5kDa and l5kDa, between 0.5kDa and MkDa, between 0.5kDa and l3kDa, between 0.5kDa and l2kDa, between 0.5kDa and l lkDa, between 0.5kDa and lOkDa, between 0.5kDa and 9kDa, between 0.5kDa and 8kDa, between 0.5kDa and 7kDa, between 0.5kDa and 6kDa, between 0.5kDa and 5kDa, between 0.5kDa and 4kDa, between 0.5kDa and 3kDa, between 0.5kDa and 2kDa, between 0.5kDa and lkDa; lkDa and MkD
  • compound is short-chain peptides produced by enzymatic hydrolysis of egg white or egg yolk using pepsin, wherein short-chain peptides have the MW no larger than 15 kDa.
  • the compound is short-chain peptides produced by enzymatic hydrolysis of egg white or egg yolk using pepsin.
  • This short-chain peptide has MW between O. lkDa and MkDa, between 0.5kDa and MkDa, between 0.5kDa and MkDa, between 0.5kDa and MkDa, between 0.5kDa and MkDa, between 0.5kDa and MkDa, between 0.5kDa and l lkDa, between 0.5kDa and lOkDa, between 0.5kDa and 9kDa, between 0.5kDa and 8kDa, between 0.5kDa and 7kDa, between 0.5kDa and 6kDa, between 0.5kDa and 5kDa, between 0.5kDa and 4kDa, between 0.5kDa and 3kDa, between 0.5kDa and 2kDa, between 0.5kDa and lkDa;
  • the polyethylene glycol (PEG) used herein may be commercially available, or prepared by methods known to one skilled in the art.
  • Typical polyethylene glycol used has a molecular weight of less than 10,000 g/mol, less than 5,000, less than 1,000, less than 500, or ranging from 100 to 400 g/mol.
  • Suitable polyethylene glycol has a formula of: , wherein ni is an integer from 2 to 10, for instance, from 3 to 5.
  • Exemplary polyethylene glycols are PEG200 (molecular weight of 200 g/mol) and PEG400 (molecular weight of 400 g/mol).
  • Sorbitan esters that can be used according to the present invention include, but are not limited to, polyoxyethylenesorbitan monolaurate (Tween 20) polyoxyethylenesorbitan monopalmitate (Tween 40), polyoxyethylenesorbitan monostearate (Tween 60),
  • the term“hydrolyzed carboxymethyl cellulose” refers to a product of a hydrolysis of carboxymethyl cellulose or a salt thereof. Wherein the product can be fully or partially hydrolyzed.
  • hydrolyzed carboxymethyl cellulose is prepared by enzymatic hydrolysis of carboxymethyl cellulose. In some embodiments, hydrolyzed carboxymethyl cellulose is prepared by acidic hydrolysis of carboxymethyl cellulose.
  • the compound is selected from the group consisting of hydrolyzed carboxymethyl cellulose (HCMC), hydrolyzed egg white (HEW), hydrolyzed egg yolk (HEY), arginine, proline, polyethylene glycol, sorbitan esters, and mixtures thereof.
  • HCMC hydrolyzed carboxymethyl cellulose
  • HW hydrolyzed egg white
  • HEY hydrolyzed egg yolk
  • arginine proline
  • proline polyethylene glycol
  • sorbitan esters and mixtures thereof.
  • the polyethylene glycol is polyethylene glycol 200
  • the compound is a peptide with strong antioxidant activity and angiotensin I-converting enzyme (ACE) inhibitory activity or a mixture thereof.
  • ACE angiotensin I-converting enzyme
  • the angiotensin converting enzyme catalyzes the conversion of inactive angiotensin I into angiotensin II, which is a strong vasoconstrictor, so one of the current therapies used in the treatment of hypertension consists of the administration of drugs inhibiting this enzyme.
  • ACE angiotensin converting enzyme
  • Several natural inhibitors of ACE have been recently described: peptides from wine (Takayanagi et al.,“Angiotensin I Converting Enzyme-Inhibitory Peptides From Wine,” Am. J. Enol. Vitic.
  • soy Wang et al.,“Hypotensive and Physiological Effect of Angiotensin Converting Enzyme Inhibitory Peptides Derived From Soy Protein on Spontaneously Hypertensive Rats,” J. Agric Food Chem.
  • Suitable peptides that can be used according to the present invention include peptides produced during hydrolysis of plant, animal, fungal, and microbial proteins.
  • Plant proteins that can be used according to the present invention include, but are not limited to, canola proteins, pea proteins, cocoa proteins, soy proteins, peptides from wine, and flaxseed proteins.
  • Animal proteins that can be used according to the present invention include, but are not limited to, chicken proteins, beef proteins, pork proteins, fish proteins, milk proteins, and egg proteins.
  • the compound is a peptide(s) produced during hydrolysis egg proteins, for example peptides produced during hydrolysis of egg proteins using pepsin.
  • the effective amount of the compound (or combination of the compounds) can be between 1 and 20% w/w, between 1 and 15% w/w, between 1 and 10% w/w, or between 1 and 5% w/w.
  • the effective amount of the compound is 1%, 2%, 3%, 4%,
  • egg yolk further comprises egg white.
  • the method prevents gelation of egg yolk.
  • the method prevents freeze induced egg yolk gelation.
  • the compound is further combined with sugar or salt.
  • the egg yolk is further mechanically treated.
  • the mechanical treatment is colloid milling or high speed mixing.
  • Colloid milling is used to reduce the particle size of a solid in suspension in a liquid, or to reduce the droplet size of a liquid suspended in another liquid. This is done by applying high levels of hydraulic shear to the process liquid. It is frequently used to increase the stability of suspensions and emulsions.
  • Suitable colloidal mills useful in carrying out the method of the present invention include Charlotte Colloid Mill (Chemicolloid Lab’s Inc., Garden City Park, NY).
  • High speed mixing e.g., homogenization using rotor-stator
  • Suitable homogenizers useful in carrying out the method of the present invention include Ultra-Turrax T rotor-stator homogenizer (Laboratory Supply Network, Inc., Atkinson, NH).
  • Gelation is thickening of egg yolk. Gelation of egg yolk can be evaluated by evaluating the changes in hardness of feeze-thawed yolk and particle distribution of the processed yolk.
  • gelation of the egg yolk is inhibited when the hardness of the egg yolk treated with the compound according to the present invention is less than 100 g, less than 90 g, less than 80 g, less than 70 g, less than 60 g, less than 50 g, less than 40 g, less than 30 g, less than 20 g, less than 15 g, less than 10 g, less than 5 g.
  • gelation of the egg yolk is inhibited when the hardness of the egg yolk treated with the compound according to the present invention is reduced by at least 5%, at least 10%, at least 20%, at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, at least 95%.
  • Fresh untreated yolk particles size ranges from 2.5-50 pm. Freezing causes a shift to larger particles ranging from 2.9-955 pm.
  • gelation of the egg yolk is inhibited when particles sizes of the egg yolk treated with the compound according to the present invention shifts the particle size distribution to ranges from 0.1-100 pm, from 0.1-90 pm, from 0.1-80 pm, from 0.1-70 pm, from 0.1-60 pm, from 0.1-50 pm, from 0.1-40 pm, from 0.1-30 pm, from 0.1-20 pm, from 0.1-10 pm.
  • Another embodiment relates to an egg yolk-containing product of the present invention.
  • Another aspect of the invention relates to an egg yolk-containing product having inhibited susceptibility to gelation resulting from freezing further comprising the compound selected from the group consisting of amino acids, hydrolyzed proteins, hydrolyzed
  • carboxymethyl cellulose carboxymethyl cellulose, polyethylene glycol, and sorbitan esters.
  • the egg-yolk containing product is used in a food or beverage product.
  • Such a food product can include one or more food additives or foodstuffs; one or more flavorants, or flavor enhancers; one or more bitter compounds; one or more sweeteners; one or more bitterants; one or more sour flavorants; one or more salty flavorants; one or more umami flavorants; one or more plant or animal products; one or more fats, oils, or emulsions; and/or one or more probiotic bacteria or supplements.
  • composition comprising egg yolk may be used include in a food product.
  • Such products may include a boiled egg itself, various food products using a boiled egg (for example, tartar sauce, prepared bread filling, and so on), various food products containing an egg as a component (for example, mayonnaise, dressing, pasta sauce, Japanese omelette, steamed egg custard, steamed egg hotchpotch, omelette, quiche, rolled omelette, noodles, fried rice, custard cream, pudding, cake, sponge cake, ice cream, egg (custard) tart, bread, crape, and so on).
  • composition comprising egg yolk may be used include in a beverage product.
  • Such products may include buttermilk, eggnog, coffee drinks, smoothies, and cocktails.
  • the composition comprising egg yolk according to the present invention can include one or more flavorants.
  • Representative flavorants include, but are not limited to, ethyl vanillin, amyl acetate, benzaldehyde, ethyl butyrate, methyl anthranilate, methyl salicylate, or fumaric acid.
  • the composition comprising egg yolk includes one or more sweeteners, sweet flavorants, or sweet taste enhancers.
  • sweeteners, sweet flavorants, or sweet taste enhancers include but are not limited to: natural or synthetic carbohydrates or carbohydrate analogues, monosaccharides, di saccharides, oligosaccharides, and polysaccharides, rare sugars, or enriched fractions of the natural sweeteners.
  • the composition comprising egg yolk may be combined with one or more artificial sweeteners.
  • artificial sweeteners may include, but are not limited to: a sulfonyl amide sweetener, e.g., selected from saccharin, sodium cyclamate and acesulfame potassium.
  • the composition comprising egg yolk may be combined with one or more bitterants, bitter flavor compounds, or bitterness-enhancing compounds.
  • the composition comprising egg yolk may be combined with one or more bitter compounds.
  • Representative bitterants, bitter flavor compounds, bitterness-enhancing compounds, and bitter compounds include but are not limited to: caffeine, denatonium benzoate, saccharin.
  • the composition comprising egg yolk may be combined with one or more acids or sour flavorants.
  • sour flavorants include but are not limited to: ascorbic acid, benzoic acid, gallic acid, glucuronic acid, adipic acid, glutaric acid, malonic acid, succinic acid, malic acid, acetic acid, lactic acid, citric acid, tartaric acid, fumaric acid, phosphoric acid, pyrophosphoric acid, tannic acid, vinegar, lemon juice, lime juice, acidic fruit juices, and acidic fruit extracts.
  • the composition comprising egg yolk may be combined with one or more salts or salt flavor enhancers.
  • Representative salts or salt flavor enhancers include, but are not limited to: mineral salts, sodium chloride, potassium chloride, magnesium chloride, ammonium chloride, sodium gluconate, sodium phosphates, glycine, L-alanine, L- valine, L-leucine, L-isoleucine, L-phenylalanine, L-tyrosine, L-glutamine, L-glutamic acid, L- asparagine, L-aspartic acid, L-serine, L-threonine, L-cysteine, L-methionine, L-proline, L-lysine, L-arginine, L-tryptophan, L-histidine, L-pyrolysine, L-pyroglutamine, L-4-trans-hydroxyproline, L-3-cis-hydroxyproline, L-homoserine, L
  • the composition comprising egg yolk may be combined with one or more umami flavor compounds or umami flavor enhancing compounds.
  • umami flavor compounds or umami flavor enhancing compounds include but are not limited to: hydrolyzed soy protein, hydrolyzed corn protein, hydrolyzed wheat protein, anchovy, fish sauce, mushrooms, oyster sauce, soy sauce, soy extract, tamari, miso powder, miso paste, kombu, nori, seaweed, tomato, vegetable powder, vegetable extract, whey, and others.
  • the composition comprising egg yolk may be combined with one or more plant or animal products.
  • the composition comprising egg yolk may be combined with one or more plant or animal products where the plant or animal product is a culinary herb or spice.
  • Representative culinary herbs and spices include but are not limited to: carrot, dehydrated carrot, onion, onion powder, onion flakes, onion extract, garlic, dehydrated garlic, garlic flakes, garlic powder, garlic extract, buttermilk, buttermilk powder, buttermilk solids, whey, whey powder, whey solids, milk, reduced fat milk, milk powder, or milk solids.
  • the composition comprising egg yolk may be combined with one or more fats, oils, or emulsions.
  • Representative fats, oils, and emulsions include but are not limited to: com oil, peanut oil, soybean oil, palm oil, coconut oil, canola oil, rapeseed oil, olive oil, safflower oil, sunflower oil, sesame oil, almond oil, beech nut oil, brazil nut oil, cashew oil, flaxseed oil, hazelnut oil, mongongo nut oil, pecan oil, pine nut oil, pistachio oil, walnut oil, grapeseed oil, chicken fat, beef fat, lamb fat, animal fat, tallowate, tallow, beef tallow, bacon fat, ham fat, suet, milk fat, olestra, stearic acid, lauric acid, linoleic acid, palmitic acid, palmitoleic acid, myristic acid, goose fat, duck fat, and oil-in water
  • the composition comprising egg yolk may be combined with one or more probiotic bacteria or supplements.
  • probiotic bacteria or supplements include but are not limited to: B. lactis, L. acidophilus, B. animalis, B. breve, or B. longum.
  • the composition comprising egg yolk may be combined with one or more starches, gums, starch-like plant extracts and materials and combinations thereof.
  • Starches that can be used in accordance with the present invention include, but are not limited to cereal starch, tuber starch, any other plant starch (such as sago starch), or any combination of any of these in any proportion.
  • Suitable cereal starches include corn starch such as instant com starch, wheat starch, rice starch, oat starch, waxy maize starch such as cook-up waxy maize starch and instant waxy maize starch, sorghum starch, waxy sorghum starch, seed starch and any combination of any of these in any proportion.
  • Suitable tuber starches including potato starch, arrowroot starch, tapioca starch, and any combination of these in any proportion.
  • Suitable gums include arabic gum, tragacanth gum, karaya gum, ghatti, guar gum such as instant, pre-hydrated guar gum, locust bean gum, xanthan gum, tamarine gum, agar-agar gum, furcellaran gum, gum acacia, and any combination of any of these in any proportion.
  • Plant extracts that can be used in accordance with the present invention include, but are not limited to pectin, arabinogalacton, psyllium, quince seed, alginates, carrageenans, and any combination of these in any proportion.
  • HCMC carboxymethyl cellulose
  • HWP hydrolyzed egg white protein
  • HYP hydrolyzed egg yolk protein
  • HCMC was prepared following the optimal conditions found by Sreenath,
  • the concentration of reducing ends of HCMC was measured using Somogyi-Nelson method (Nelson,“A Photometric Adaptation of the Somogyi Method for the Determination of Glucose,” Journal of Biological Chemistry l53(2):375-380 (1944), which is hereby incorporated by reference in its entirety).
  • a quantification standard curve was established using serial dilutions of 1 mg/mL solution of glucose The standard solutions and samples were measured at 520 nm, and the absorbance of the CMC and HCMC samples was interpolated into the standard curve to determine the concentration of free reducing ends in both samples.
  • the average molecular weight of the HCMC was estimated to be 2 9 kDa based on the inverse relationship between the obtained amount of reducing ends and molecular weights before and after hydrolysis.
  • Egg yolk was defatted prior to hydrolysis by extracting lipids using the method of Folch et al.,“A Simple Method for the Isolation and Purification of Total Lipids From Animal Tissues,” J. Biol. Chem. 226(l):497-509 (1957), which is hereby incorporated by reference in its entirety.
  • Fresh egg yolk was mixed in 2 parts of 2: 1 (v/v) chloroform -methanol solution in a shaking incubator for 30 minutes at the ambient temperature. The mixture was vacuum-filtered using No.2 Whatman paper, and the filter cake was air dried for 12 hours to remove solvent.
  • the egg protein was dispersed in deionized water at 10 g protein (dry weight)/L water and denatured in 90°C water bath for 15 minutes.
  • the pH of the denatured dispersion was adjusted to 2 using 2 M hydrochloric acid solution.
  • the hydrolysis reaction was performed for 3 hours after adding pepsin at a selected concentration, and the temperature and pH were maintained at 45°C and 2, respectively. Inactivation of pepsin was achieved by increasing the solution pH to 7 with 2 M sodium hydroxide solution.
  • the hydrolysates were centrifuged at 4,000g for 15 minutes and the supernatant was collected and lyophilized.
  • fresh yolk was processed with a rotor- stator homogenizer and a colloid mill prior to freezing.
  • rotor-stator homogenizer fresh yolk was processed at 8,000, 13,500, and 24,000 RPM for 90 seconds.
  • the shear rates were calculated to be 13,299, 22,443, and 39,898 s 1 , respectively.
  • DSC differential scanning calorimetry
  • T m Melting temperature
  • DH enthalpy
  • the amount of freezable water in yolk was calculated following the method by Wakamatu et al.,“On Sodium Chloride Action in the Gelation Process Of Low Density Lipoprotein (LDL) from Hen Egg Yolk,” Journal of Food Science 48(2):507-512 (1983), which is hereby incorporated by reference in its entirety.
  • the exothermic or endothermic heat was divided by the corresponding heat of fusion of pure water (242.88 J/g for cooling and 320.62 J/g for heating). Freezable water content was reported as the average of the exothermic and endothermic freezable water values per gram of solid.
  • Particle size distributions of fresh and frozen-thawed yolk were measured by laser diffraction (LD) method using Malvern Mastersizer 2000 particle size analyzer with Hydro 2000 MU large volume wet sample dispersion unit (Malvern Instruments, Inc., Worchestershore, UK) following the method by Au et al.,“Determination of the Gelation Mechanism of Freeze- Thawed Hen Egg Yolk,” Journal of Agricultural and Food Chemistry 63(46): l0170-10180 (2015), which is hereby incorporated by reference in its entirety. All samples were diluted at a sample: deionized water ratio of 1 : 1.5 (v/v) and mixed for 1.5 hours on a stir plate until being homogeneous.
  • LD laser diffraction
  • Protein surface hydrophobicity (So) of the fresh and frozen-thawed yolk mixtures was determined using l-anilino-8-naphthalene sulfonate (ANS) as a hydrophobic probe (Wu et al.,“Hydrophobicity, Solubility, and Emulsifying Properties of Soy Protein Peptides Prepared by Papain Modification and Ultrafiltration,” Journal of the American Oil Chemists' Society 75(7):845-850 (1998), which is hereby incorporated by reference in its entirety).
  • the protein was serially diluted with deionized water to obtain protein concentrations ranging from 0 000675 to 0.01925%.
  • FI fluorescence intensity
  • concentration was calculated by least square linear regression and used as the surface hydrophobicity.
  • SAS Statistical Analysis System Institute Inc.
  • Cary NC
  • ANOVA One-way analysis of variance tests were conducted, and significance of difference (p ⁇ 0.05) was calculated using Tukey’s HSD (honest significant difference) test.
  • Proline also proved to be a very effective gelation inhibitor.
  • the hardness of proline-treated yolk was reduced by 87% compared to the yolk without additive. When added at 10% concentration, it inhibited gelation almost completely and the yolk maintained its fresh texture.
  • proline is relatively expensive compared to salt and sugar, and the amount of proline as an additive is not allowed to exceed 4.2% of the total protein content in the food (Food Additives Permitted for Direct Addition to Food for Human Consumption, ⁇ 172.320 (2017), which is hereby incorporated by reference in its entirety).
  • Figures 4A-G show the hardness of frozen-thawed yolk treated with different combinations of additives. An apparent linear increase in hardness was observed as proline concentration is reduced and HCMC concentration is increased, indicating that proline and FICMC do not prevent gelation synergistically (Figure 4A). Similar trends were observed in treatments involving HCMC-HEY and HCMC-HEW ( Figures 4B-4C).
  • HCMC might have been inactivated and the gelation inhibition was mostly due to salt, as shown through the decreasing hardness with increasing salt content.
  • Figures 5A-5C show how colloid milling affected gelation and particle size distribution.
  • the milling was able to significantly reduce gelation, and the addition of 2.5% proline and 5% HCMC to the milled sample was effective to inhibit gelation comparable to the performance of 10% salt ( Figures 5A-5C).
  • Colloid milling was reported to decrease the degree of gelation of frozen yolk; the smaller the clearance of the mill, the less the gelation.
  • Sucrose showed a completely different mechanism in inhibiting gelation. Its addition lowered the viscosity of the unfrozen yolk and 10% sucrose yolk was completely fluid.
  • Sugars have been commonly used as stabilizers to protect proteins from degradation during lyophilization and frozen storage.
  • Two main hypotheses have been proposed to explain the stabilization mechanism of sugar: the“water substitution” hypothesis and the“glass dynamics” hypothesis. In the“water substitution” hypothesis, stabilizers form hydrogen bonds at specific sites on protein surface and thus substitute for the stabilization function of water that is lost during freezing induced dehydration.
  • CMC an anionic water soluble polymer derived from cellulose
  • FIG. 7A shows how HCMC affected particle size distribution in fresh and frozen-thawed yolk.
  • the measured yolk particles were relatively smaller compared to fresh yolk, and this supports the statement that HCMC forms electrostatic interaction with proteins, thus increasing the net negative charge and repulsive forces between proteins (Huan et al., “Influence of the Molecular Weight of Carboxymethylcellulose On Properties and Stability of Whey Protein-Stabilized Oil-In-Water Emulsions,” Journal of Dairy Science 99(5):3305-33 l5 (2016), which is hereby incorporated by reference in its entirety). Gelation still caused the distribution to shift towards larger particles, but not to the extent of the untreated frozen-thawed yolk. Protein surface hydrophobicity test also confirmed this mechanism.
  • HCMC -treated yolk had a significantly higher surface hydrophobicity than untreated yolk before freezing ( Figure 7B).
  • the negative net charges kept proteins apart in aqueous dispersion that made it easier for the hydrophobic ANS probe to access the hydrophobic region on the yolk proteins.
  • the melting transition and freezable water were also significantly reduced due to the high solubility of HCMC.
  • proline forms hydrophobic stacking in aqueous solution through the formation of hydrogen bonding between the imino group of proline with the negatively charged carboxyl group of the adjacent proline molecule.
  • the carboxyl groups can also form hydrogen bonding with the solvent water molecules (Samuel et al.,“Proline Inhibits Aggregation During Protein Refolding,” Protein Science 9(2):344-352 (2000), which is hereby incorporated by reference in its entirety).
  • This amphiphilic proline assembly suppresses aggregation by shielding the hydrophobic, aggregation-prone region of the proteins (Kumat et al.,“The Role of Proline in the Prevention of Aggregation During Protein Folding in vitro,” IUBMB Life 46(3):509-5 l7 (1998), which is hereby incorporated by reference in its entirety).
  • Hen egg white and egg yolk proteins were enzymatically hydrolyzed using pepsin for production of short-chain peptides.
  • Enzymatic hydrolysis is known to increase the value of food proteins by modifying their physical and nutritional properties.
  • Other than reducing molecular weight, increasing the number of ionizable groups, and exposing the initially buried hydrophobic groups, enzymatic hydrolysis improves the solubility of proteins and modulates their surface or interfacial properties such as stabilization of emulsions and foams (Foegeding et al.,“Food Protein Functionality: A Comprehensive Approach,” Food Hydrocolloids, 25: 1853- 1864 (2011), which is hereby incorporated by reference in its entirety).
  • Peptides from collagen source inhibited ice recrystallization at molecular weight range of 0.6-2.7 kDa (Wang et al,“Ice-Structuring Peptides Derived From Bovine Collagen,” Journal of Agricultural and Food Chemistry 57(l2):550l- 5509 (2009), which is hereby incorporated by reference in its entirety). It is accepted that the inhibition mechanism involves binding of these peptides to the ice-liquid interface, which primarily involves hydrogen bonding. As measured by SDS-PAGE, the peptides produced from egg white and yolk hydrolysis were no larger than 15 kDa. Future work will further identify the optimal size of the egg peptides for yolk gelation inhibition.
  • Novel yolk gelation inhibitors that can potentially replace salt or sugar were identified and assessed.
  • HEW, HEY, HCMC, and proline have been proven to effectively inhibit gelation of frozen-thawed yolk through different mechanisms.
  • These additives can be used in combination, or with sugar and colloid milling for further reduction in gelation.
  • hydrolyzed egg proteins prevented gelation as the typically used 10% salt or sugar, and they were effective at an addition level of 5%.
  • the different mechanisms of gelation inhibition are discussed according to this observation. There is great potential for using such egg derived ingredients to replace salt and sugar to effectively prevent yolk gelation in commercial yolk freezing storage operations.

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Abstract

La présente invention concerne une méthode permettant d'inhiber la gélification du jaune d'œuf résultant de la congélation-décongélation. Cette méthode comprend le traitement du jaune d'œuf avec une quantité efficace d'un composé sélectionné dans le groupe constitué par les acides aminés, les protéines hydrolysées, la carboxyméthylcellulose hydrolysée, le polyéthylène glycol et les esters de sorbitan, afin d'améliorer les propriétés de gélification du jaune d'œuf. La présente invention concerne également un produit contenant du jaune d'œuf dont la susceptibilité à la gélification liée à la congélation a été inhibée, comprenant le composé sélectionné dans le groupe constitué par les acides aminés, les protéines hydrolysées, la carboxyméthylcellulose hydrolysée, le polyéthylène glycol et les esters de sorbitan.
PCT/US2018/033473 2018-05-18 2018-05-18 Inhibition de la gélification du jaune d'œuf au cours de la congélation WO2019221752A1 (fr)

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Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1870269A (en) * 1930-08-16 1932-08-09 Frosted Foods Co Inc Egg product and method of producing the same
US2142511A (en) * 1935-11-23 1939-01-03 Emulsol Corp Egg product
US2395587A (en) * 1943-04-17 1946-02-26 Ind Patents Corp Egg product
US3408207A (en) * 1967-02-02 1968-10-29 Howell Foods Corp Process for making a freezable egg food product
US20050186321A1 (en) * 2004-01-30 2005-08-25 Nancy Ullrich Frozen heat and serve egg patty

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US1870269A (en) * 1930-08-16 1932-08-09 Frosted Foods Co Inc Egg product and method of producing the same
US2142511A (en) * 1935-11-23 1939-01-03 Emulsol Corp Egg product
US2395587A (en) * 1943-04-17 1946-02-26 Ind Patents Corp Egg product
US3408207A (en) * 1967-02-02 1968-10-29 Howell Foods Corp Process for making a freezable egg food product
US20050186321A1 (en) * 2004-01-30 2005-08-25 Nancy Ullrich Frozen heat and serve egg patty

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
PRIMACELLA ET AL.: "Effect of food additives on egg yolk gelation induced by freezing", FOOD CHEMISTRY, vol. 263, 21 April 2018 (2018-04-21), pages 142 - 150, XP085402032, DOI: 10.1016/j.foodchem.2018.04.071 *

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