US20060225610A1 - Edible phosphoprotein film - Google Patents
Edible phosphoprotein film Download PDFInfo
- Publication number
- US20060225610A1 US20060225610A1 US10/531,350 US53135003A US2006225610A1 US 20060225610 A1 US20060225610 A1 US 20060225610A1 US 53135003 A US53135003 A US 53135003A US 2006225610 A1 US2006225610 A1 US 2006225610A1
- Authority
- US
- United States
- Prior art keywords
- film
- film according
- casein
- mixture
- cross linking
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
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- 108010089430 Phosphoproteins Proteins 0.000 title claims abstract description 47
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- 239000012505 Superdex™ Substances 0.000 description 1
- 102100027208 T-cell antigen CD7 Human genes 0.000 description 1
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 1
- XEFQLINVKFYRCS-UHFFFAOYSA-N Triclosan Chemical compound OC1=CC(Cl)=CC=C1OC1=CC=C(Cl)C=C1Cl XEFQLINVKFYRCS-UHFFFAOYSA-N 0.000 description 1
- 239000005862 Whey Substances 0.000 description 1
- 102000007544 Whey Proteins Human genes 0.000 description 1
- 108010046377 Whey Proteins Proteins 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- YGCFIWIQZPHFLU-UHFFFAOYSA-N acesulfame Chemical class CC1=CC(=O)NS(=O)(=O)O1 YGCFIWIQZPHFLU-UHFFFAOYSA-N 0.000 description 1
- 229960005164 acesulfame Drugs 0.000 description 1
- 238000007605 air drying Methods 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 229940035676 analgesics Drugs 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000000730 antalgic agent Substances 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000843 anti-fungal effect Effects 0.000 description 1
- 230000003610 anti-gingivitis Effects 0.000 description 1
- 230000000845 anti-microbial effect Effects 0.000 description 1
- 230000002882 anti-plaque Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 229940121375 antifungal agent Drugs 0.000 description 1
- 229940125715 antihistaminic agent Drugs 0.000 description 1
- 239000000739 antihistaminic agent Substances 0.000 description 1
- 239000008122 artificial sweetener Substances 0.000 description 1
- 235000021311 artificial sweeteners Nutrition 0.000 description 1
- 239000000605 aspartame Substances 0.000 description 1
- IAOZJIPTCAWIRG-QWRGUYRKSA-N aspartame Chemical compound OC(=O)C[C@H](N)C(=O)N[C@H](C(=O)OC)CC1=CC=CC=C1 IAOZJIPTCAWIRG-QWRGUYRKSA-N 0.000 description 1
- 235000010357 aspartame Nutrition 0.000 description 1
- 229960003438 aspartame Drugs 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 239000003139 biocide Substances 0.000 description 1
- 230000001680 brushing effect Effects 0.000 description 1
- VTYYLEPIZMXCLO-UHFFFAOYSA-L calcium carbonate Substances [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 description 1
- 229910000019 calcium carbonate Inorganic materials 0.000 description 1
- FNAQSUUGMSOBHW-UHFFFAOYSA-H calcium citrate Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O.[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O FNAQSUUGMSOBHW-UHFFFAOYSA-H 0.000 description 1
- 239000001354 calcium citrate Substances 0.000 description 1
- 159000000007 calcium salts Chemical class 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 229920001525 carrageenan Polymers 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 238000005266 casting Methods 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 230000007073 chemical hydrolysis Effects 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 235000015218 chewing gum Nutrition 0.000 description 1
- 229960003260 chlorhexidine Drugs 0.000 description 1
- 150000003841 chloride salts Chemical class 0.000 description 1
- 239000010500 citrus oil Substances 0.000 description 1
- 239000010634 clove oil Substances 0.000 description 1
- 238000004040 coloring Methods 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 239000000686 essence Substances 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 229960002217 eugenol Drugs 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 150000002222 fluorine compounds Chemical class 0.000 description 1
- 235000002864 food coloring agent Nutrition 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 229940046240 glucomannan Drugs 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 125000005456 glyceride group Chemical group 0.000 description 1
- 238000000227 grinding Methods 0.000 description 1
- 235000001050 hortel pimenta Nutrition 0.000 description 1
- 239000000416 hydrocolloid Substances 0.000 description 1
- 239000008172 hydrogenated vegetable oil Substances 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 229940076522 listerine Drugs 0.000 description 1
- 229960005015 local anesthetics Drugs 0.000 description 1
- 239000007937 lozenge Substances 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L magnesium chloride Substances [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 229910001425 magnesium ion Inorganic materials 0.000 description 1
- 238000004890 malting Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 239000001683 mentha spicata herb oil Substances 0.000 description 1
- 229960001047 methyl salicylate Drugs 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 235000021096 natural sweeteners Nutrition 0.000 description 1
- 229940126701 oral medication Drugs 0.000 description 1
- 238000000643 oven drying Methods 0.000 description 1
- 238000010979 pH adjustment Methods 0.000 description 1
- 239000005022 packaging material Substances 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 108010024951 plastein Proteins 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920000223 polyglycerol Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000011045 prefiltration Methods 0.000 description 1
- MFDFERRIHVXMIY-UHFFFAOYSA-N procaine Chemical compound CCN(CC)CCOC(=O)C1=CC=C(N)C=C1 MFDFERRIHVXMIY-UHFFFAOYSA-N 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 238000000734 protein sequencing Methods 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000012146 running buffer Substances 0.000 description 1
- 230000035807 sensation Effects 0.000 description 1
- 235000019615 sensations Nutrition 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 235000002639 sodium chloride Nutrition 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 239000001587 sorbitan monostearate Substances 0.000 description 1
- 235000011076 sorbitan monostearate Nutrition 0.000 description 1
- 229940035048 sorbitan monostearate Drugs 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 235000019721 spearmint oil Nutrition 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 239000000021 stimulant Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 235000019408 sucralose Nutrition 0.000 description 1
- BAQAVOSOZGMPRM-QBMZZYIRSA-N sucralose Chemical compound O[C@@H]1[C@@H](O)[C@@H](Cl)[C@@H](CO)O[C@@H]1O[C@@]1(CCl)[C@@H](O)[C@H](O)[C@@H](CCl)O1 BAQAVOSOZGMPRM-QBMZZYIRSA-N 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 230000000475 sunscreen effect Effects 0.000 description 1
- 239000000516 sunscreening agent Substances 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 239000000454 talc Substances 0.000 description 1
- 229910052623 talc Inorganic materials 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 235000013337 tricalcium citrate Nutrition 0.000 description 1
- 229910000391 tricalcium phosphate Inorganic materials 0.000 description 1
- 235000019731 tricalcium phosphate Nutrition 0.000 description 1
- 229940078499 tricalcium phosphate Drugs 0.000 description 1
- 229960003500 triclosan Drugs 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229910021642 ultra pure water Inorganic materials 0.000 description 1
- 239000012498 ultrapure water Substances 0.000 description 1
- 229960005486 vaccine Drugs 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 238000009463 water soluble packaging Methods 0.000 description 1
- 239000009637 wintergreen oil Substances 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y203/00—Acyltransferases (2.3)
- C12Y203/02—Aminoacyltransferases (2.3.2)
- C12Y203/02013—Protein-glutamine gamma-glutamyltransferase (2.3.2.13), i.e. transglutaminase or factor XIII
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/01—Hydrolysed proteins; Derivatives thereof
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/04—Animal proteins
- A23J3/08—Dairy proteins
- A23J3/10—Casein
-
- 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
- A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
- A23L27/70—Fixation, conservation, or encapsulation of flavouring agents
- A23L27/79—Fixation, conservation, or encapsulation of flavouring agents in the form of films
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23P—SHAPING OR WORKING OF FOODSTUFFS, NOT FULLY COVERED BY A SINGLE OTHER SUBCLASS
- A23P20/00—Coating of foodstuffs; Coatings therefor; Making laminated, multi-layered, stuffed or hollow foodstuffs
- A23P20/20—Making of laminated, multi-layered, stuffed or hollow foodstuffs, e.g. by wrapping in preformed edible dough sheets or in edible food containers
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K6/00—Preparations for dentistry
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/0053—Mouth and digestive tract, i.e. intraoral and peroral administration
- A61K9/006—Oral mucosa, e.g. mucoadhesive forms, sublingual droplets; Buccal patches or films; Buccal sprays
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/02—Stomatological preparations, e.g. drugs for caries, aphtae, periodontitis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
Definitions
- the present invention generally relates to films, and more particularly to edible films. More specifically, the present invention relates to edible film compositions comprising a phosphoprotein preparation, and to methods of malting the same.
- Oral cleansing and breath freshening may be difficult or inconvenient at times, depending on the nature of the breath freshening desired and the situation in which the breath freshening must be carried out.
- Methods such as brushing, flossing and gargling using various devices and compositions are common oral care practices that are suitable for carrying out in the privacy of one's home.
- U.S. Pat. No. 4,562,020 describes a self supporting glucan film prepared from an aqueous solution comprising pullulan or elsinan. These films are said to be useable as an edible, water-soluble packaging material.
- U.S. Pat. No. 4,623,394 describes edible films comprising pullulan and heteromannan, which are said to exhibit controlled disintegrability under hydrous conditions.
- U.S. Pat. No. 4,851,394 discloses an edible film based on the reaction product of a polyhydric alcohol and glucomannan and optionally other natural polysaccharides. These films are said to have desirable properties such as water resistance, heat resistance and strength.
- European patent publication 1,008,343 A1 discloses a film preparation for oral drug delivery and said to have rapid solubility, comprising a drug, an edible polymer and a saccharide.
- U.S. patent application publication No. 2002/0150544 A1 discloses an edible film containing therapeutic agents and/or breath freshening agents for use in the oral cavity, comprising a mixture of a water-soluble polymer, a polyalcohol, a cosmetically and/or pharmaceutically active agent such as a breath freshener, and a flavor.
- U.S. patent application publication No. 2003/008008 A1 discloses edible films having an antimicrobial effect, comprising a water-soluble polymer such as pullulan, and an essential oil selected from thymol, methyl salicylate, eucalyptol and menthol.
- U.S. patent application publication No. 2003/0035841 A1 describes an edible film for oral mucoadhesion, comprising at least three film-forming agents, namely a naltodextrin, a hydrocolloid and a filler, but not including pullulan.
- U.S. patent application publication No. 20021131990 A1 also discloses pullulan-free edible films, comprising a film forming agent (such as carageenan), a bulk filler agent and a plasticizing agent.
- a film forming agent such as carageenan
- the present invention provides a film comprising:
- the film is edible.
- the film is substantially soluble.
- the cations are divalent.
- the source of the cations comprises a substantially water-insoluble salt of the cations.
- the cations comprise calcium ions.
- the source of calcium ions comprises calcium phosphate.
- some or all of the calcium phosphate is in the form of calcium. enzymatic hydrolysis of acid casein, rennet casein or a caseinate.
- the enzyme is trypsin, and the partial hydrolysis has been carried out at a pH of from about 7 to about 8.
- the partial cross linking has been cared out enzymatically, using transglutaminase, preferably at a pH of from about 7 to about 8.
- the edible film farther comprises one or more emulsifiers.
- the emulsifier comprises a citric acid ester of mono- and diglycerides, such as that commercially available under the trade name Lamegin 609ZE.
- the edible film may further include one or more additional agents such as flavoring or breath freshening agents, sweeteners, coloring agents, pH control agents and stabilizers.
- the edible film may further include one or more active agents selected from the group consisting of an oral care agent, a pharmaceutical or veterinary agent, a nutraceutical agent, a salivary stimulant agent, a vitamin, a mineral and combinations thereof
- the present invention provides a process of producing an edible film, the process comprising the steps of:
- the mixture includes water.
- the processing includes the steps of applying the mixture to a surface followed by drying to form the film.
- the processing comprises extruding the mixture to form a film.
- the present invention provides a mixture capable of being processed to produce an edible film, the mixture comprising (a) a phosphoprotein preparation, wherein the phosphoprotein preparation has been obtained by partially cross linking a partial hydrolysate of casein or a caseinate, (b) a source of one or more physiologically acceptable cations, and (c) a plasticizer.
- the applicants have surprisingly found that thin, edible films, having desirable organoleptic and physical properties, and which dissolve rapidly in the mouth, can be prepared from certain phosphoproteins when combined with a suitable cation.
- the present invention therefore provides novel films, preferably edible films, and methods of making and using them.
- the films of the present invention have a number of applications. For example, they may be used to deliver breath fresheners or other oral care agents. Alternatively or additionally, they may act as carriers for pharmaceutical or veterinary agents, nutraceutical agents, salivary stimulant agents, vitamins, minerals, or combinations thereof
- the edible films of the present invention may be used as a readily soluble and/or edible coating for foods.
- the films may be used as a vehicle to apply active agents topically to the skin.
- the films of the present invention although still dissolving rapidly in the mouth, at least in certain preferred embodiments, have a lower solubility than certain pullulan-based films that are currently available. This in turn means that at least in certain preferred embodiments, the edible films of the present invention have the advantage of “grabbing” less in the mouth and providing a relatively clean mouth feel on dissolution.
- the film of the present invention are preferably substantially soluble.
- substantially soluble means that the film as a whole disintegrates and dissolves readily in the mouth of a consumer.
- some components of the film, in particular salt components may not dissolve completely in a technical sense, as some undissolved material of a very small particle size may remain. Such small particles will generally be undetectable to the consumer.
- the edible films of the present invention comprise a phosphoprotein preparation, a source of one or more physiologically acceptable cations, and a plasticizer.
- the phosphoprotein preparations suitable for use in the edible films of the present invention may be obtained by partially cross linking a partial hydrolysate of casein or a caseinate, that is, casein or a caseinate in which some, but not all, of the peptide bonds have been hydrolyzed.
- cross linking when used in the context of partially cross linking a partial hydrolysate of casein or a caseinate, means the formation of intermolecular covalent bonds between the amino acid residues of the casein molecules and/or casein molecule fragments comprising the partial hydrolysate.
- the intermolecular covalent bonds comprise bonds between glutamine and lysine residues, ie glutamylalysyl covalent bonds. It will also be appreciated that some intramolecular cross linking, ie between amino acid residues on the same casein molecule or casein fragment, is likely to occur.
- partial when used in the context of “partial cross linking”, means that not all of the amino acid residues are cross-linked, ie that some non-cross linked amino acid residues will remain following the cross linking reaction.
- the degree of partial cross linking is expressed herein in terms of micromoles of cross links per gram of protein.
- the casein used to prepare the partial hydrolysate may be in any form; acid casein, rennet casein or a caseinate may all be used.
- chemical hydrolysis is by no means excluded, it is preferred that the partial hydrolysis is carried out enzymatically, in aqueous solution.
- Suitable enzymes for performing the partial hydrolysis include proteases, such as trypsin and chymotpsin. It is however particularly preferred that the enzyme used is trypsin, such as bovine derived or porcine pancreatic trypsin.
- the partial hydrolysis should be carried out at a temperature and pH appropriate to the enzyme being used.
- the partial hydrolysis may conveniently be carried out at a pH of between about 7 and about 8, and at a temperature of about 37° C.
- the casein will be present as a caseinate, eg sodium caseinate, depending on the buffer used in the reaction solution.
- the reaction should be carried out for a sufficient period of time and under appropriate conditions, eg enzyme and casein concentrations, to allow the casein to be partially hydrolyzed, ie for some, but not all, of the peptide bonds to be hydrolyzed.
- the reaction may conveniently be terminated or at least substantially terminated, by inactivating the enzyme, for example by heating the reaction mixture to a temperature which will denature the enzyme, eg to about 80° C. It is not critical that the hydrolysis reaction be completely terminated, provided the partial cross liking reaction (as discussed below) is commenced once the desired degree of hydrolysis has been achieved. That is, a minor amount of hydrolysis may still continue while the partial cross linking reaction is being carried out.
- the level of partial hydrolysis of the casein is in the range of about 0.5% to 10%, ie 0.5% to 10% of the peptide bonds in the casein are hydrolyzed. It is more preferred that the level of partial hydrolysis is in the range of about 2% to about 8%, such as about 3% to about 6%.
- the degree of hydrolysis may be determined by methods known to those skilled in the art, conveniently by the TNBS (2,4,6tiinitrobenzene sulfonic acid) method.
- the degree of hydrolysis is such that about 15% or less of the casein or caseinate is rendered insoluble at pH 7, by the partial hydrolysis.
- a partially hydrolyzed casein suitable for use in the films of the invention may be prepared by first solubilising a 10% isoelectric precipitated casein solution with NaOH to pH 7 at 5sOC. The solution is then cooled to 37° C, and a porcine pancreatic trypsin preparation added at about 0.01% w/w casein and incubated for 15 minutes.
- a suitable porcine pancreatic trypsin preparation is that commercially available as Novo.4500K, molecular weight 23,400 Da, activity 4500 USP units/mg.
- the partially hydrolyzed casein Once the partially hydrolyzed casein has been prepared, it is then partially Cross linked to form a phosphoprotein preparation suitable for use in the films of the present invention.
- the partial cross linking may be carried out either enzymatically or chemically. It is however preferred that the partial cross linking is carried out enzymatically; conveniently using either of the enzymes lysyl oxidase or transglutaminase,
- the enzyme transglutaminase is used, and that the partial cross linking reaction is carried out at a pH of between about 7 and about 8.
- the reaction is carried out under suitable conditions and for a time sufficient to allow the desired degree of cross linking to take place. It is preferred that the reaction be carried out under conditions such that the degree of cross linking in the resulting phosphoprotein preparation comprises about 10 ⁇ mol or more cross links per gram of protein, more preferably between about 10 and about 250 ⁇ mol/g protein, more preferably between about 50 and 160 ⁇ mol/g protein, such as between about 110 and 150 ⁇ mol/g protein.
- the degree of partial cross linking in terms of the quantity of glutamyl/lysl bonds, may conveniently be determined by high performance liquid chromatography (HPLC), by carrying out a proteolytic digestion of the cross-linked proteins using suitable enzymes, conveniently pronase, leucine aminopeptidase, prolidase and carboxypeptidase, followed by HPLC of the proteolytic digest and quantification of the ⁇ -( ⁇ -Glutamyl)lysine (G-L) peak.
- HPLC high performance liquid chromatography
- the reaction may conveniently be terminated by inactivation of the enzyme, typically by heating the reaction mixture to a temperature sufficient to denature the enzyme, for example to about 80° C. for about 5 minutes. It is also generally preferred that, following completion of the partial cross linking and deactivation of the enzyme, the resulting phosphoprotein-containing solution is dialyzed or diafiltered to remove any remaining low molecular weight peptides and salts, conveniently using a membrane with a molecular weight cutoff of from about 10,000 Da to about 14,000 Da.
- the purified phosphoprotein containing solution may be freeze dried or spray dried to obtain the phosphoprotein preparation in a solid form.
- transglutaminase Any commercially available source of transglutaminase may be used to carry out the partial cross linking reaction.
- a suitable enzyme is a 1% transglutaminase preparation commercially available from Ajinomoto Co. as Activa MP.
- a phosphoprotein preparation suitable for use in the films of the present invention may be obtained by treating a partially hydrolyzed casein (prepared as described above) with a transglutaminase preparation (Activa MP) added at a ratio of 4.5% w/w casein and incubating the reaction mixture at 40° C. for 18 hours.
- Activa MP transglutaminase preparation
- the plastein reaction which is an enzymatic reaction known to those skilled in the art
- the cross linking may also be carried out between tyrosine residues using peroxidase and hydrogen peroxide.
- partial cross linking is carried out enzymatically, partial cross linking by chemical means using a suitable reagent is by no means excluded.
- a bifunctional aldehyde such as glutaraldehyde may be used.
- the phosphoprotein preparations as described above are able to bind and thus solubilise significant quantities of cation salts, particularly salts of calcium and other divalent cations. Moreover, the phosphoprotein preparations have a higher solubility than unmodified casein. The applicants have further surprisingly found that by combining the phosphoprotein preparations with a source of a cation, the solubility of the phosphoprotein preparation can be controlled in a way which renders it capable forming a stable, thin film having the desirable properties discussed above.
- the films of the invention therefore include a source of one or more physiologically acceptable cations.
- the cation is divalent, and is preferably selected from the group consisting of calcium, zinc and magnesium ions.
- the source of the cation may conveniently be an inorganic or organic salt, such as a phosphate, citrate or chloride. It is however preferred that the salt is a salt that is substantially insoluble in water.
- the cations are calcium ions.
- the source of calcium ions preferably comprises calcium phosphate, more preferably in the form of calcium hydroxyapatite.
- the source of calcium ions comprises natural milk calcium, such as that available from New Zealand.
- ALAMIN® which comprises calcium, phosphate, and also protein, lactose, fat, moisture, sodium, potassium and chloride, in the following typical proportions: Total mineral content 70% (w/w): 28% calcium and 48% phosphate Protein (N ⁇ 6.38) 7% Lactose 4% Fat 1% Free moisture 3% Bound moisture 8% Calcium 28,000 mg/100 g Phosphorus 16,000 mg/100 g Sodium 400 mg/100 g Potassium 300 mg/100 g Chloride 100 mg/100 g
- Natural milk calcium phosphate In natural milk calcium phosphate, the calcium phosphate is generally regarded as being in the form of calcium hydroxyapatite. Natural milk calcium phosphate may be obtained by methods known in the art, typically by classifying and pasteurizing acid whey permeate, cooling and ultrafiltering the permeate, followed by heating, pH adjustment and holding at the elevated temperature such that the minerals including calcium phosphate will be precipitated, and recovery of the precipitate.
- Another suitable source of natural milk calcium phosphate is the product available under the trade mark Lactoval® from DMV International.
- calcium phosphate in the form of tricalcium phosphate may be used.
- Embodiments of the invention in which the source of calcium ions comprises natural milk calcium phosphate are particularly preferred. These preferred films demonstrate accelerated dissolution and getaway in the mouth. Without wishing to be bound by any theory, it is believed that the insoluble portion of the natural milk calcium phosphate may also act in a filler capacity, helping weaken the structure of the film and thus aid disintegration.
- the films may comprise another calcium source, such as calcium citrate or calcium chloride.
- the films it is generally preferred that the films also include a filler, such as talc.
- the relative proportions of the source of cations and the phosphoprotein preparation in thee edible films of the present invention will vary, depending on a number of factors. These include the properties, notably the solubility and cation-binding properties, of the particular phosphoprotein preparation being used, the type of cation and salt being used, and the desired properties of the edible film in question, such as its desired thickness and solubility. These in turn will depend on the intended end use of the film, for example whether it is to be used as a stand-alone film for delivery of breath-freshener, flavor or other active agent, or whether it is to be used for some other application such as an edible coating or packaging for a food.
- the calcium or other cation source should be included in the film formulations in an amount sufficient to aid in the formation of a flexible and cohesive film.
- the optimum amount of cation to be included may be readily determined by a person skilled in the art without undue experimentation.
- the ratio (w/w) calcium ions-phosphoprotein may be in the range of about 0.05:1 to about 0.0136:1; the ratio (w/w) hydroxyapatite:phosphoprotein may be in the range of about 0.2:1 to about 0.92: 1, and the ratio (w/w) natural milk calcium phosphate:phosphoprotein may be in tie range of about 0.3:1 to about 1.3:1.
- the edible films of the present invention may also desirably include a plasticizer (softener).
- the plasticizer may be any plasticizer suitable for inclusion in an edible film, such as a polyhydric alcohol, for example glycerol, sorbitol (preferably in combination with glycerol), polyethylene glycol, or propylene glycol, or hydrogenated starch hydrolysates or corn syrups.
- the plasticizer comprises glycerol.
- the plasticizer may conveniently constitute between about 10% and 25%, more preferably between about 15 to 18%, of the dry weight of the filmL
- the edible films of the present invention may also desirably include one or more emulsifiers.
- the emulsifiers ray be any suitable natural or synthetic food-grade emulsifiers.
- the emulsifier can include mono- and diacyl glycerides, citric acid esters of mono- and diglycerides, partially hydrogenated vegetable oils, lecithin, fatty acids, polyglycerol esters, polyethylene sorbitan esters, propylene glycol, sorbitan. monopalmitate, sorbitan monostearate, or soxbitan tristearate, and other like emulsifiers.
- the emulsifier(s) may conveniently constitute between 0.5% and 3% of the dry weight of the film.
- the film may also include one or more additional agents such as flavorings or breath freshening agents, sweeteners, coloring agents, pH control agents and stabilizers.
- additional agents such as flavorings or breath freshening agents, sweeteners, coloring agents, pH control agents and stabilizers.
- Flavoring or breath freshening agents may include, for example, essential oils, synthetic flavors or mixtures including oils derived from plants and fruits such as citrus oil fruit essences such as orange, peppermint oil, spearmint oil, other mint oils, clove oils, oil of wintergreen, anise and the like, flavor oils with germ killing properties such as menthol, eucalyptol, eugenol, thymol, and germ killing agents like that found within the brand name product Listerine®, and combinations thereof.
- essential oils synthetic flavors or mixtures including oils derived from plants and fruits such as citrus oil fruit essences such as orange, peppermint oil, spearmint oil, other mint oils, clove oils, oil of wintergreen, anise and the like
- flavor oils with germ killing properties such as menthol, eucalyptol, eugenol, thymol, and germ killing agents like that found within the brand name product Listerine®, and combinations thereof.
- flavoring or breath freshening agent added will depend on the properties of the particular agent, but in general the flavoring or breath freshening agent may constitute between about 2% and 10% of the dry weight of the film
- suitable sweeteners include natural sweeteners such as sucrose, dextrose and maltose, and artificial sweeteners such as sucralose, aspartame, and salts of acesulfame such as Ace K.
- Suitable colorings include food colors and dyes suitable for food applications, such as FD&C lakes and dyes.
- pH control agents examples include orally acceptable buffers.
- the edible film may include one or more active agents such as an oral care agent, a salivary stimulant agent, a pharmaceutical or veterinary agent, a nutraceutical agent, a vitamin, a mineral, and combinations thereof
- Oral care agents that may be incorporated into the films of the present invention include phosphates and fluorides, and anti-plaque/anti-gingivitis agents such as chlorohexidine, acetylpyridinium chloride and triclosan; and salivary stimulants.
- Pharmaceutical, veterinary and nutraceutical agents, and vitamins and minerals which may be incorporated within the edible film compositions of the present invention include those agents which are suitable for oral consumption and can be placed within film formulations.
- the films may be used as delivery vectors for vaccines, antibiotics, analgesics, antihistamines, bacteriocins or local anaesthetics such as Novocain.
- the films may also be used to deliver therapeutics orally to small animals and other animals such as cows, pigs, deer and horses.
- the edible films of the present invention may be prepared by processing a mixture comprising a phosphoprotein preparation as described above, a source of one or more physiologically acceptable cations and a plasticizer, in a suitable manner to form a film; and, optionally, drying the film to reduce the moisture content to a desired level.
- the mixture includes water.
- the films may be prepared by casting.
- the method of preparation may conveniently comprise the steps of combining the dry ingredients of the film formulation with a blend of the water and other liquid ingredients. It is preferred that the dry ingredients are blended together before being added slowly to-the blend of the liquid ingredients. When preparing the blend of the liquid ingredients, it may also be desirable to heat this gently to assist in dissolving of the emulsifier (if present). The ingredients should be mixed thoroughly. It may be desirable to add fierier water to adjust the consistency of the solution during mixing, in order to obtain a solution of a consistency that can be spread onto a support for drying, and/or to adjust the thickness of the film.
- the solution may optionally be emulsified and/or degassed
- the pH of the solution should preferably be maintained at about 6 to about 8, more preferably at about 7.2 to 7.8, and still more preferably at about 7.5.. This may conveniently be achieved by adding a suitable pH control agent, such as sodium hydroxide.
- the solution may then be poured or otherwise applied on to a suitable support, such as a dry glass plate, or to a surface on which it is intended to form a coating.
- a suitable support such as a dry glass plate
- the films of the present invention may be either self-supporting, or they will adhere when hot to a structural surface such as paper, and thus may serve as a coating if desired.
- the films may be dried in any suitable manner, including air-drying, oven drying, reflectance window drying or roller drying.
- the films of the present invention may be prepared by extruding a mixture comprising the film ingredients.
- it may not be essential to include a drying step following extrusion of the film, depending on the proportion of water that is included in the extrusion mixture and the final moisture content of the extruded film.
- the films may conveniently be prepared by combining the liquid ingredients, slowly adding them to a mixture of the dry ingredients, adjusting the pH (for example to about 7.5) so that the mixture forms a thermoplastic mass, cooling the mixture so that the mass becomes crumbly, and grinding the mass to a powder which is suitable for extrusion.
- the desired thickness of the films on the present invention will vary, depending on the intended use of the film
- the thickness of edible films of the invention may desirably be in the range of about 30 to about 80 ⁇ m, such as about 40-50 ⁇ m, for example around 43 to 47 ⁇ m.
- the thickness of the film may be controlled by adjusting various parameters, including the proportion of plasticizer, the proportion of water in the dry product, the method used for spreading and drying, the initial thickness of the wet film, and, to a certain extent, the pH.
- the dry ingredients (phosphoprotein, Alamin®, and Ace-K) were blended.
- the phosphoprotein was prepared as described in Example 3.
- liquid ingredients emulsifier, flavor, glycerol and water
- emulsifier emulsifier, flavor, glycerol and water
- the pH was adjusted to 7.5 with 4M NaOH.
- the solution was spread onto a dry glass plate (0.25mm thickness), and dried at 100-110° C. for about 4-5 minutes.
- the plate was left to rehydrate at room temperature, then the film peeled off the plate using blade.
- the molecular weight profiles of the partially hydrolysed preparation was determined by gel filtration as follows. A 1% protein solution was prepared in 6M Urea, with 50 mM sodium phosphate at pH 7.5 as the buffer. This solution was centrifuged at 10 000 ⁇ g for 10 minutes and passed through a 0.2 ⁇ m filter. A sample volume of 500 ⁇ l injected into the 100 ⁇ l sample loop of a Pharmacia FPLC fitted with a Superdex 200 10/30HR column. The running buffer used was 6 M Urea, with 50 mM sodium phosphate at pH 7.5 and flow rate of 0.5 my/min. Detection was by UV absorption (280-nm). The protein absorption curve was integrated and arbitrarily divided into the following four molecular weight groupings:
- the pH was re-adjusted to 7.0, and transglutaminase (1% commercial preparation, Activa MP, Ajinomoto Co) added at a ratio of 4.5% wlw casein and incubated for 15 hours (temperature at the end of incubation was 32° C.).
- the solution was heated to 80° C and held for 5 minutes.
- the solution was diluted to 1000 L and cooled to 5° C.
- the solution was ultrafiltered until a final concentration of 20% solids was achieved and then spray diied.
- the molecular weight material greater than 30,000 Da was increased by 100% and the nunber of crossline s in the protein was 92 ⁇ mol/g.
- Extruded films were prepared using the following formulation on a Brabender Twin Screw extruder. Ingredients Extrusion 1 Extrusion 2 Protein MAP112 (Example 3) 32.40 30.0 Milk derived calcium phosphate 32.40 30.0 Ace-K 0.99 1.0 Emulsifier 1.62 1.5 Flavour Peppermint Oil 6.48 6.0 Glycerol 16.20 13.0 Water 9.91 18.5 100.0 100.0 Method of Preparation
- the liquid ingredients water, glycerol, peppermint oil and emulsifier
- the dry mix Protein MAP112, Milk derived calcium phosphate and Acesulfame K
- the pH was adjusted to 7.5 with 4M NaOH.
- the resulting mixture formed a thermoplastic mass that was crumbly at temperatures below 18° C.
- the mixture was cooled to 0° C. and ground to a powder.
- Barrel temperature profile (from feed end) Section 1 50° C. Section 2 60° C. Section 3 65° C. Section 4 75° C. Nozzle 80° C.
- the crumble was fed into hopper and extruded as a thin film. As the film was exited the nozzle it was picked up by strips of paper (silicon backed, 0.25 ⁇ m thickness 2 m length). The paper speed was varied to achieve films with thicknesses ranging from 40 ⁇ m to 150 ⁇ m The films were packed in foil laminate bags.
- ⁇ -( ⁇ -Glutamyl)lysine G-L and trifluoroacetic acid (TPA, protein sequencing grade), Prolidase (porcine, kidney), Leucine aminopeptidase and cytosol from hog kidney, Carboxypeptidase A (bovine pancreas) and Pronase ( Streptomyces griseus ) and TRIS [Tris(hydroxymethyl)aninomethane] were purchased from Sigma Chem Co. (Sydney, Australia). Acetonitrile (HPLC grade) was purchased from Biolab (Christchurch, New Zealand).
- a 48-50 mg aliquot of protein sample was weighed in a glass test tube (total volume 15 mL). A crystal of thymol and 2 ml of 0.2 M Tris (H 8.0, HCl) was added, the solution vortexed and then incubated at 40° C. for 1 h to allow the dispersion of the protein. An aliquot of Pronase (0.4 U/mg protein) was added to the mixture which was then incubated at 37° C. for 24 h. The pronase digestion was continued for a fisher 24 h by the addition of another equal sized aliquot of pronase. After inactivation of pronase by heating at 100° C.
- the HPLC system consisted of a Dionex GP40 gradient pump solvent delivery system connected to an ICI Instruments 1210 UV/Vis detector. Data was captured via an ITNS Acquisition Board and analysed using the AZUR chromatography software Version 1.1. The samples (100 ⁇ l) were separated on an Inertsil ODS-2 column (5 Em, 150 ⁇ 7.6 mm) (Phenomenex, Auckland, New Zealand) connected to a guard column (C 18 ODS, 4 mm ⁇ 3.0 mm ID)(Phenomenex) and a 2 Fun prefilter. Analysis was- performed at 2.5° C. The mobile phases were 0.1% TFA (v/v)(solvent A) and acetonitrile containing 0.1% TPA (v/v) (solvent B). Tfhe solvent program was as follows: 100% solvent A for 20 nn 0% to 100% solvent B from 20 to 25 min, 100% solvent B from 25 to 50 min. The detector wavelength was set at 210 nm and the flow rate was 1.0 ml/min.
- the characteristics of the phosphoproteins used in the preparations were as follows: Lot 102: degree of hydrolysis (DH) 8.8%, degree of cross linking IS0punol/g protein; MAP 106: DH 4.4%, degree of cross linking 155pmol/g protein, MAP 109: DH 5.7%, degree of cross linking 155 ⁇ mol/g protein.
- liquid ingredients emulsifier, flavor, glycerol and water
- the mixture was heated gently to 30-40° C. as required, to dissolve the emulsifier.
- the pH was adjusted to 7.5 with 4M NaOH.
- the solution was spread onto a dry glass plate (0.25 mm thickness), and dried at 100-110° C. for about 4-5 minutes.
- the plate was left to rehydrate at room temperature and then the film peeled off the plate using a blade.
- the films were prepared as per Example 6.
- Samples were prepared as either 0.1% or 1% protein (w/v) solutions in distilled water.
- a 100 ⁇ l aliquot of sample was added to 800 ⁇ l of 0.2125 M sodium phosphate buffer, pH 8.20.
- 800 pi 0.1% TNBS reagent was added, and the reagents were mixed well, wrapped in foil and incubated at 50° C. in a covered water-bath. After exactly 60 minutes the reaction was terminated by the addition of 1600 ⁇ l of 100 mM HCl and the samples left to cool to room temperature for 30 minutes before reading absorbance against a buffer/TNBS blank at 340 ⁇ m.
- the films of the present invention have a number of applications. For example, they may be used to deliver a breath freshener or other oral care agent Alternatively or additionally, they may act as a carrier for a pharmaceutical or veterinary agent, a nutraceutical agent, a salivay stimulant agent, a vitamin, a mineral or combinations thereof.
- the edible films of the present invention may be used as a readily soluble and/or edible coating for foods such as fruit or confectionery products. They may also be used in food product labeling, such as cheese labeling.
- a further application is in the preparation of novel confections such as tongue tattoos.
- the films may be used to as a vehicle to apply active agents topically to the skin.
- active agents for example, sunscreen (SPF) agents, burn recovery agents, Herpes simplex remedies, and topical antifungal disease agents may be incorporated in the films of the present invention.
- SPDF sunscreen
- burn recovery agents Herpes simplex remedies
- topical antifungal disease agents may be incorporated in the films of the present invention.
- the films may be used in diagnostic kits, particularly in immunology, or in forensic applications.
- the edible films of the present invention have the advantage of “grabbing” less in the mouth and providing a relatively clean mouth feel on dissolution, as compared to certain currently available pullulan-based films.
- the quick getaway in the mouth of the films of the present invention also gives them potential for use in sudden flavor release.
Abstract
The invention provides a film comprising a phosphoprotein preparation, wherein the phosphoprotein preparation has been obtained by partially cross linking a partial hydrolysate of casein or a caseinate, a source of one or more physiologically acceptable cations, and a plasticizer. The film is preferably edible and substantially soluble. In particularly preferred embodiments, the source of one or more physiologically acceptable cations comprises natural milk calcium phosphate, and the plasticizer is glycerol.
Description
- The present invention generally relates to films, and more particularly to edible films. More specifically, the present invention relates to edible film compositions comprising a phosphoprotein preparation, and to methods of malting the same.
- Oral cleansing and breath freshening may be difficult or inconvenient at times, depending on the nature of the breath freshening desired and the situation in which the breath freshening must be carried out. Methods such as brushing, flossing and gargling using various devices and compositions are common oral care practices that are suitable for carrying out in the privacy of one's home.
- However, such devices and compositions are less convenient to use away from the home where bathroom facilities may be unavailable or unsanitary. Less obtrusive oral care products have been developed for use in these situations, such as breath-freshening chewing gums, lozenges, mouth sprays, and edible films.
- A variety of edible films are known in the art.
- For example, U.S. Pat. No. 4,562,020 describes a self supporting glucan film prepared from an aqueous solution comprising pullulan or elsinan. These films are said to be useable as an edible, water-soluble packaging material.
- U.S. Pat. No. 4,623,394 describes edible films comprising pullulan and heteromannan, which are said to exhibit controlled disintegrability under hydrous conditions.
- U.S. Pat. No. 4,851,394 discloses an edible film based on the reaction product of a polyhydric alcohol and glucomannan and optionally other natural polysaccharides. These films are said to have desirable properties such as water resistance, heat resistance and strength.
- European patent publication 1,008,343 A1 discloses a film preparation for oral drug delivery and said to have rapid solubility, comprising a drug, an edible polymer and a saccharide.
- U.S. patent application publication No. 2002/0150544 A1 discloses an edible film containing therapeutic agents and/or breath freshening agents for use in the oral cavity, comprising a mixture of a water-soluble polymer, a polyalcohol, a cosmetically and/or pharmaceutically active agent such as a breath freshener, and a flavor.
- U.S. patent application publication No. 2003/008008 A1 discloses edible films having an antimicrobial effect, comprising a water-soluble polymer such as pullulan, and an essential oil selected from thymol, methyl salicylate, eucalyptol and menthol.
- U.S. patent application publication No. 2003/0035841 A1 describes an edible film for oral mucoadhesion, comprising at least three film-forming agents, namely a naltodextrin, a hydrocolloid and a filler, but not including pullulan.
- U.S. patent application publication No. 20021131990 A1 also discloses pullulan-free edible films, comprising a film forming agent (such as carageenan), a bulk filler agent and a plasticizing agent.
- However, despite the existence of rapidly soluble edible films in the prior art, there is still room for improvement in such films. For example, the available pullulan-based films have such high solubility that on contact with the consumer's mouth they may impart an undesirable “grabbing” sensation as they dissolve. Accordingly, the mouth feel on dissolution of such films may not be as clean as is ideal.
- It is an object of the present invention to provide an edible film which goes at least some way towards overcoming the above disadvantage, or at least to provide the public with an a useful choice.
- Accordingly, in a first aspect the present invention provides a film comprising:
-
- (a) a phosphoprotein preparation, wherein the phosphoprotein preparation has been obtained by partially cross linking a partial hydrolysate of casein or a caseinate,
- (b) a source of one or more physiologically acceptable cations, and
- (c) a plasticizer.
- In preferred embodiments, the film is edible.
- In preferred embodiments, the film is substantially soluble.
- In preferred embodiments, the cations are divalent.
- In preferred embodiments, the source of the cations comprises a substantially water-insoluble salt of the cations.
- In preferred embodiments, the cations comprise calcium ions.
- In particularly preferred embodiments, the source of calcium ions comprises calcium phosphate.
- In certain preferred embodiments, some or all of the calcium phosphate is in the form of calcium. enzymatic hydrolysis of acid casein, rennet casein or a caseinate.
- In preferred embodiments, the enzyme is trypsin, and the partial hydrolysis has been carried out at a pH of from about 7 to about 8.
- In preferred embodiments, the partial cross linking has been cared out enzymatically, using transglutaminase, preferably at a pH of from about 7 to about 8.
- In preferred embodiments, the edible film farther comprises one or more emulsifiers. In one embodiment, the emulsifier comprises a citric acid ester of mono- and diglycerides, such as that commercially available under the trade name Lamegin 609ZE.
- In further embodiments, the edible film may further include one or more additional agents such as flavoring or breath freshening agents, sweeteners, coloring agents, pH control agents and stabilizers.
- In certain embodiments, the edible film may further include one or more active agents selected from the group consisting of an oral care agent, a pharmaceutical or veterinary agent, a nutraceutical agent, a salivary stimulant agent, a vitamin, a mineral and combinations thereof In a further aspect, the present invention provides a process of producing an edible film, the process comprising the steps of:
-
- (a) processing a mixture comprising (a) a phosphoprotein preparation, wherein the phosphoprotein preparation has been obtained by partially cross lining a partial hydrolysate of casein or a caseinate, (b) a source of one or more physiologically acceptable cations, and (c) a plasticizer, to form a film; and
- (b) optionally, drying the film to reduce the moisture content to a desired level.
- In preferred embodiments, the mixture includes water.
- In certain preferred embodiments,.the processing includes the steps of applying the mixture to a surface followed by drying to form the film.
- In other preferred embodiments, the processing comprises extruding the mixture to form a film.
- In still a further aspect, the present invention provides a mixture capable of being processed to produce an edible film, the mixture comprising (a) a phosphoprotein preparation, wherein the phosphoprotein preparation has been obtained by partially cross linking a partial hydrolysate of casein or a caseinate, (b) a source of one or more physiologically acceptable cations, and (c) a plasticizer.
- Although the invention is broadly as defined above, it is not limited thereto and also includes embodiments of which the following detailed description provides examples.
- The applicants have surprisingly found that thin, edible films, having desirable organoleptic and physical properties, and which dissolve rapidly in the mouth, can be prepared from certain phosphoproteins when combined with a suitable cation. The present invention therefore provides novel films, preferably edible films, and methods of making and using them. The films of the present invention have a number of applications. For example, they may be used to deliver breath fresheners or other oral care agents. Alternatively or additionally, they may act as carriers for pharmaceutical or veterinary agents, nutraceutical agents, salivary stimulant agents, vitamins, minerals, or combinations thereof In other embodiments, the edible films of the present invention may be used as a readily soluble and/or edible coating for foods. In still further embodiments, the films may be used as a vehicle to apply active agents topically to the skin.
- The films of the present invention, although still dissolving rapidly in the mouth, at least in certain preferred embodiments, have a lower solubility than certain pullulan-based films that are currently available. This in turn means that at least in certain preferred embodiments, the edible films of the present invention have the advantage of “grabbing” less in the mouth and providing a relatively clean mouth feel on dissolution.
- Accordingly, the film of the present invention are preferably substantially soluble. As used herein, the term “substantially soluble” means that the film as a whole disintegrates and dissolves readily in the mouth of a consumer. However, it will be understood that some components of the film, in particular salt components, may not dissolve completely in a technical sense, as some undissolved material of a very small particle size may remain. Such small particles will generally be undetectable to the consumer.
- As defined above, the edible films of the present invention comprise a phosphoprotein preparation, a source of one or more physiologically acceptable cations, and a plasticizer.
- The phosphoprotein preparations suitable for use in the edible films of the present invention may be obtained by partially cross linking a partial hydrolysate of casein or a caseinate, that is, casein or a caseinate in which some, but not all, of the peptide bonds have been hydrolyzed.
- As used herein, the term “cross linking”, when used in the context of partially cross linking a partial hydrolysate of casein or a caseinate, means the formation of intermolecular covalent bonds between the amino acid residues of the casein molecules and/or casein molecule fragments comprising the partial hydrolysate. Preferably, the intermolecular covalent bonds comprise bonds between glutamine and lysine residues, ie glutamylalysyl covalent bonds. It will also be appreciated that some intramolecular cross linking, ie between amino acid residues on the same casein molecule or casein fragment, is likely to occur.
- The term “partial”, when used in the context of “partial cross linking”, means that not all of the amino acid residues are cross-linked, ie that some non-cross linked amino acid residues will remain following the cross linking reaction.
- The degree of partial cross linking is expressed herein in terms of micromoles of cross links per gram of protein.
- The casein used to prepare the partial hydrolysate may be in any form; acid casein, rennet casein or a caseinate may all be used. Although chemical hydrolysis is by no means excluded, it is preferred that the partial hydrolysis is carried out enzymatically, in aqueous solution. Suitable enzymes for performing the partial hydrolysis include proteases, such as trypsin and chymotpsin. It is however particularly preferred that the enzyme used is trypsin, such as bovine derived or porcine pancreatic trypsin.
- The partial hydrolysis should be carried out at a temperature and pH appropriate to the enzyme being used. For example, if bovine derived trypsin is used, the partial hydrolysis may conveniently be carried out at a pH of between about 7 and about 8, and at a temperature of about 37° C. It will also be appreciated that at this pH, the casein will be present as a caseinate, eg sodium caseinate, depending on the buffer used in the reaction solution.
- The reaction should be carried out for a sufficient period of time and under appropriate conditions, eg enzyme and casein concentrations, to allow the casein to be partially hydrolyzed, ie for some, but not all, of the peptide bonds to be hydrolyzed. When partial hydrolysis has been achieved, the reaction may conveniently be terminated or at least substantially terminated, by inactivating the enzyme, for example by heating the reaction mixture to a temperature which will denature the enzyme, eg to about 80° C. It is not critical that the hydrolysis reaction be completely terminated, provided the partial cross liking reaction (as discussed below) is commenced once the desired degree of hydrolysis has been achieved. That is, a minor amount of hydrolysis may still continue while the partial cross linking reaction is being carried out.
- It is generally preferred that the level of partial hydrolysis of the casein is in the range of about 0.5% to 10%, ie 0.5% to 10% of the peptide bonds in the casein are hydrolyzed. It is more preferred that the level of partial hydrolysis is in the range of about 2% to about 8%, such as about 3% to about 6%.
- The degree of hydrolysis may be determined by methods known to those skilled in the art, conveniently by the TNBS (2,4,6tiinitrobenzene sulfonic acid) method.
- It is also preferred that the degree of hydrolysis is such that about 15% or less of the casein or caseinate is rendered insoluble at pH 7, by the partial hydrolysis.
- Purely by way of example, a partially hydrolyzed casein suitable for use in the films of the invention may be prepared by first solubilising a 10% isoelectric precipitated casein solution with NaOH to pH 7 at 5sOC. The solution is then cooled to 37° C, and a porcine pancreatic trypsin preparation added at about 0.01% w/w casein and incubated for 15 minutes. A suitable porcine pancreatic trypsin preparation is that commercially available as Novo.4500K, molecular weight 23,400 Da, activity 4500 USP units/mg. Once the partial hydrolysis has been carried out, enzyme inactivation may be achieved by heating to 80° C. and holding for 5 minutes.
- Once the partially hydrolyzed casein has been prepared, it is then partially Cross linked to form a phosphoprotein preparation suitable for use in the films of the present invention.
- The partial cross linking may be carried out either enzymatically or chemically. It is however preferred that the partial cross linking is carried out enzymatically; conveniently using either of the enzymes lysyl oxidase or transglutaminase,
- It is particularly preferred that the enzyme transglutaminase is used, and that the partial cross linking reaction is carried out at a pH of between about 7 and about 8. The reaction is carried out under suitable conditions and for a time sufficient to allow the desired degree of cross linking to take place. It is preferred that the reaction be carried out under conditions such that the degree of cross linking in the resulting phosphoprotein preparation comprises about 10 μmol or more cross links per gram of protein, more preferably between about 10 and about 250 μmol/g protein, more preferably between about 50 and 160 μmol/g protein, such as between about 110 and 150 μmol/g protein.
- The degree of partial cross linking, in terms of the quantity of glutamyl/lysl bonds, may conveniently be determined by high performance liquid chromatography (HPLC), by carrying out a proteolytic digestion of the cross-linked proteins using suitable enzymes, conveniently pronase, leucine aminopeptidase, prolidase and carboxypeptidase, followed by HPLC of the proteolytic digest and quantification of the ε-(γ-Glutamyl)lysine (G-L) peak.
- Again, once the partial cross linking reaction has been carried out, the reaction may conveniently be terminated by inactivation of the enzyme, typically by heating the reaction mixture to a temperature sufficient to denature the enzyme, for example to about 80° C. for about 5 minutes. It is also generally preferred that, following completion of the partial cross linking and deactivation of the enzyme, the resulting phosphoprotein-containing solution is dialyzed or diafiltered to remove any remaining low molecular weight peptides and salts, conveniently using a membrane with a molecular weight cutoff of from about 10,000 Da to about 14,000 Da. The purified phosphoprotein containing solution may be freeze dried or spray dried to obtain the phosphoprotein preparation in a solid form.
- Any commercially available source of transglutaminase may be used to carry out the partial cross linking reaction. By way of example, a suitable enzyme is a 1% transglutaminase preparation commercially available from Ajinomoto Co. as Activa MP.
- Purely by way of example, a phosphoprotein preparation suitable for use in the films of the present invention may be obtained by treating a partially hydrolyzed casein (prepared as described above) with a transglutaminase preparation (Activa MP) added at a ratio of 4.5% w/w casein and incubating the reaction mixture at 40° C. for 18 hours. Alternatively, the plastein reaction (which is an enzymatic reaction known to those skilled in the art) may be used. The cross linking may also be carried out between tyrosine residues using peroxidase and hydrogen peroxide.
- As discussed above, although it is preferred that the partial cross linking is carried out enzymatically, partial cross linking by chemical means using a suitable reagent is by no means excluded. For example, a bifunctional aldehyde such as glutaraldehyde may be used.
- The applicants have surprisingly found that the phosphoprotein preparations as described above are able to bind and thus solubilise significant quantities of cation salts, particularly salts of calcium and other divalent cations. Moreover, the phosphoprotein preparations have a higher solubility than unmodified casein. The applicants have further surprisingly found that by combining the phosphoprotein preparations with a source of a cation, the solubility of the phosphoprotein preparation can be controlled in a way which renders it capable forming a stable, thin film having the desirable properties discussed above. Without wishing to be bound by any theory, it is believed that by adding a source of a cation, such as a calcium salt, the water-binding capacity of the phosphoprotein is decreased, thereby enabling the formation of a tin, stable film which dissolves rapidly in the mouth.
- The films of the invention therefore include a source of one or more physiologically acceptable cations. It is preferred that the cation is divalent, and is preferably selected from the group consisting of calcium, zinc and magnesium ions. The source of the cation may conveniently be an inorganic or organic salt, such as a phosphate, citrate or chloride. It is however preferred that the salt is a salt that is substantially insoluble in water.
- It is particularly preferred that the cations are calcium ions. The source of calcium ions preferably comprises calcium phosphate, more preferably in the form of calcium hydroxyapatite. In particularly preferred embodiments, the source of calcium ions comprises natural milk calcium, such as that available from New Zealand. Milk Products Ltd under the trade name ALAMIN®, which comprises calcium, phosphate, and also protein, lactose, fat, moisture, sodium, potassium and chloride, in the following typical proportions:
Total mineral content 70% (w/w): 28% calcium and 48% phosphate Protein (N × 6.38) 7% Lactose 4% Fat 1% Free moisture 3% Bound moisture 8% Calcium 28,000 mg/100 g Phosphorus 16,000 mg/100 g Sodium 400 mg/100 g Potassium 300 mg/100 g Chloride 100 mg/100 g - In natural milk calcium phosphate, the calcium phosphate is generally regarded as being in the form of calcium hydroxyapatite. Natural milk calcium phosphate may be obtained by methods known in the art, typically by classifying and pasteurizing acid whey permeate, cooling and ultrafiltering the permeate, followed by heating, pH adjustment and holding at the elevated temperature such that the minerals including calcium phosphate will be precipitated, and recovery of the precipitate.
- Another suitable source of natural milk calcium phosphate is the product available under the trade mark Lactoval® from DMV International.
- Alternatively, calcium phosphate in the form of tricalcium phosphate may be used.
- Embodiments of the invention in which the source of calcium ions comprises natural milk calcium phosphate are particularly preferred. These preferred films demonstrate accelerated dissolution and getaway in the mouth. Without wishing to be bound by any theory, it is believed that the insoluble portion of the natural milk calcium phosphate may also act in a filler capacity, helping weaken the structure of the film and thus aid disintegration.
- In other embodiments, the films may comprise another calcium source, such as calcium citrate or calcium chloride. In these embodiments it is generally preferred that the films also include a filler, such as talc.
- The relative proportions of the source of cations and the phosphoprotein preparation in thee edible films of the present invention will vary, depending on a number of factors. These include the properties, notably the solubility and cation-binding properties, of the particular phosphoprotein preparation being used, the type of cation and salt being used, and the desired properties of the edible film in question, such as its desired thickness and solubility. These in turn will depend on the intended end use of the film, for example whether it is to be used as a stand-alone film for delivery of breath-freshener, flavor or other active agent, or whether it is to be used for some other application such as an edible coating or packaging for a food. However, in general terms, the calcium or other cation source should be included in the film formulations in an amount sufficient to aid in the formation of a flexible and cohesive film. The optimum amount of cation to be included may be readily determined by a person skilled in the art without undue experimentation.
- By way of example, in embodiments of the invention in which the cation is calcium and the cation source is natural milk calcium phosphate as described above, the ratio (w/w) calcium ions-phosphoprotein may be in the range of about 0.05:1 to about 0.0136:1; the ratio (w/w) hydroxyapatite:phosphoprotein may be in the range of about 0.2:1 to about 0.92: 1, and the ratio (w/w) natural milk calcium phosphate:phosphoprotein may be in tie range of about 0.3:1 to about 1.3:1.
- The edible films of the present invention may also desirably include a plasticizer (softener). The plasticizer may be any plasticizer suitable for inclusion in an edible film, such as a polyhydric alcohol, for example glycerol, sorbitol (preferably in combination with glycerol), polyethylene glycol, or propylene glycol, or hydrogenated starch hydrolysates or corn syrups. In preferred embodiments the plasticizer comprises glycerol.
- The plasticizer may conveniently constitute between about 10% and 25%, more preferably between about 15 to 18%, of the dry weight of the filmL
- Although not critical, the edible films of the present invention may also desirably include one or more emulsifiers. The emulsifiers ray be any suitable natural or synthetic food-grade emulsifiers. For example, the emulsifier can include mono- and diacyl glycerides, citric acid esters of mono- and diglycerides, partially hydrogenated vegetable oils, lecithin, fatty acids, polyglycerol esters, polyethylene sorbitan esters, propylene glycol, sorbitan. monopalmitate, sorbitan monostearate, or soxbitan tristearate, and other like emulsifiers.
- The emulsifier(s) may conveniently constitute between 0.5% and 3% of the dry weight of the film.
- Depending on the intended application of the film, it may also include one or more additional agents such as flavorings or breath freshening agents, sweeteners, coloring agents, pH control agents and stabilizers.
- Flavoring or breath freshening agents that may be used may include, for example, essential oils, synthetic flavors or mixtures including oils derived from plants and fruits such as citrus oil fruit essences such as orange, peppermint oil, spearmint oil, other mint oils, clove oils, oil of wintergreen, anise and the like, flavor oils with germ killing properties such as menthol, eucalyptol, eugenol, thymol, and germ killing agents like that found within the brand name product Listerine®, and combinations thereof. The amount of flavoring or breath freshening agent added will depend on the properties of the particular agent, but in general the flavoring or breath freshening agent may constitute between about 2% and 10% of the dry weight of the film Suitable sweeteners include natural sweeteners such as sucrose, dextrose and maltose, and artificial sweeteners such as sucralose, aspartame, and salts of acesulfame such as Ace K.
- Suitable colorings include food colors and dyes suitable for food applications, such as FD&C lakes and dyes.
- Examples of pH control agents include orally acceptable buffers.
- In certain embodiments, the edible film may include one or more active agents such as an oral care agent, a salivary stimulant agent, a pharmaceutical or veterinary agent, a nutraceutical agent, a vitamin, a mineral, and combinations thereof
- Oral care agents that may be incorporated into the films of the present invention include phosphates and fluorides, and anti-plaque/anti-gingivitis agents such as chlorohexidine, acetylpyridinium chloride and triclosan; and salivary stimulants.
- Pharmaceutical, veterinary and nutraceutical agents, and vitamins and minerals which may be incorporated within the edible film compositions of the present invention include those agents which are suitable for oral consumption and can be placed within film formulations.
- For example, the films may be used as delivery vectors for vaccines, antibiotics, analgesics, antihistamines, bacteriocins or local anaesthetics such as Novocain. The films may also be used to deliver therapeutics orally to small animals and other animals such as cows, pigs, deer and horses.
- In general terms, the edible films of the present invention may be prepared by processing a mixture comprising a phosphoprotein preparation as described above, a source of one or more physiologically acceptable cations and a plasticizer, in a suitable manner to form a film; and, optionally, drying the film to reduce the moisture content to a desired level.
- In preferred embodiments, the mixture includes water.
- In some embodiments, the films may be prepared by casting. The method of preparation may conveniently comprise the steps of combining the dry ingredients of the film formulation with a blend of the water and other liquid ingredients. It is preferred that the dry ingredients are blended together before being added slowly to-the blend of the liquid ingredients. When preparing the blend of the liquid ingredients, it may also be desirable to heat this gently to assist in dissolving of the emulsifier (if present). The ingredients should be mixed thoroughly. It may be desirable to add fierier water to adjust the consistency of the solution during mixing, in order to obtain a solution of a consistency that can be spread onto a support for drying, and/or to adjust the thickness of the film. The solution may optionally be emulsified and/or degassed The pH of the solution should preferably be maintained at about 6 to about 8, more preferably at about 7.2 to 7.8, and still more preferably at about 7.5.. This may conveniently be achieved by adding a suitable pH control agent, such as sodium hydroxide.
- The solution may then be poured or otherwise applied on to a suitable support, such as a dry glass plate, or to a surface on which it is intended to form a coating. The films of the present invention may be either self-supporting, or they will adhere when hot to a structural surface such as paper, and thus may serve as a coating if desired.
- The films may be dried in any suitable manner, including air-drying, oven drying, reflectance window drying or roller drying.
- In alternate preferred embodiments, the films of the present invention may be prepared by extruding a mixture comprising the film ingredients. In this embodiment, it may not be essential to include a drying step following extrusion of the film, depending on the proportion of water that is included in the extrusion mixture and the final moisture content of the extruded film. The films may conveniently be prepared by combining the liquid ingredients, slowly adding them to a mixture of the dry ingredients, adjusting the pH (for example to about 7.5) so that the mixture forms a thermoplastic mass, cooling the mixture so that the mass becomes crumbly, and grinding the mass to a powder which is suitable for extrusion.
- The desired thickness of the films on the present invention will vary, depending on the intended use of the film However, the thickness of edible films of the invention may desirably be in the range of about 30 to about 80 μm, such as about 40-50 μm, for example around 43 to 47 μm. The thickness of the film may be controlled by adjusting various parameters, including the proportion of plasticizer, the proportion of water in the dry product, the method used for spreading and drying, the initial thickness of the wet film, and, to a certain extent, the pH.
- The invention will now be explained in more detail with reference to the following examples, which are given for illustration of the invention and are not intended to be limiting thereof.
-
Ingredients % adjusted %1 Phosphoprotein (MAP112) 30 18.75 Alamin ® 30 18.75 Ace-K 1 0.625 Emulsifier - Lamegin 609ZE 1.5 0.935 Flavor - Peppermint Oil 6 3.75 Glycerol 15 9.38 Water 16.5 47.8
1Extra water was added to solutions to enable spreading on glass plates for drying.
Method of Preparation: - The dry ingredients (phosphoprotein, Alamin®, and Ace-K) were blended. The phosphoprotein was prepared as described in Example 3.
- The liquid ingredients (emulsifier, flavor, glycerol and water) were blended. The mixture was heated gently to 30-40° C. as required, to dissolve the emulsifier.
- The dry ingredients were added slowly to the liquids, stiring until all ingredients were well mixed Extra water was added to solutions to enable spreading on glass plates for drying.
- The pH was adjusted to 7.5 with 4M NaOH.
- The solution was spread onto a dry glass plate (0.25mm thickness), and dried at 100-110° C. for about 4-5 minutes. The plate was left to rehydrate at room temperature, then the film peeled off the plate using blade.
-
Ingredients % adjusted %1 Phosphoprotein (MAP112) 30 18.75 Alamin 30 18.75 Ace-K 1 0.625 Emulsifier - Lamegin 609ZE 1.5 0.935 Flavor - Peppermint Oil 6 3.75 Glycerol 13 8.125 Water 18.5 49.065
1Extra water was added to solutions to enable spreading on glass plates for drying.
- An edible film was prepared using the preparative method as described above for Example 1.
- Preparation of a Phosphoprotein (MAP 112)
- Tryptic Hydrolysis
- Fifty-five kilograms of sodium caseinate was dispersed in 50° C. deionised water so that a final concentration of 522 L was achieved. The solution was cooled to 37° C., the pH adjusted to 7.06 with NaOH and porcine derived trypsin (Novo.4500K, molecular weight 23,400 Da, activity 4500 USP units/mg) added at 0.01% w/w casein and incubated for five minutes. The solution was heated to 80° C. over 15 minutes, held for four minutes and cooled to 45° C.
- The molecular weight profiles of the partially hydrolysed preparation was determined by gel filtration as follows. A 1% protein solution was prepared in 6M Urea, with 50 mM sodium phosphate at pH 7.5 as the buffer. This solution was centrifuged at 10 000×g for 10 minutes and passed through a 0.2 μm filter. A sample volume of 500 μl injected into the 100 μl sample loop of a Pharmacia FPLC fitted with a Superdex 200 10/30HR column. The running buffer used was 6 M Urea, with 50 mM sodium phosphate at pH 7.5 and flow rate of 0.5 my/min. Detection was by UV absorption (280-nm). The protein absorption curve was integrated and arbitrarily divided into the following four molecular weight groupings:
- 1) greater than about 30,000 Daltons
- 2) less than about 30,000 Daltons and greater than about 21,000 Daltons
- 3) less than about 21,000 Daltons and greater than about 12,000 Daltons
- 4) less than about 12,000 Daltons.
Molecular weight profile after hydrolysis Molecular weight range Percentage ≧30,000 10.7 <30,000, ≧21,000 57.8 <21,000, ≧12,000 15.7 <12,000 15.8
Transglutaminase Treatment - The pH was re-adjusted to 7.0, and transglutaminase (1% commercial preparation, Activa MP, Ajinomoto Co) added at a ratio of 4.5% wlw casein and incubated for 15 hours (temperature at the end of incubation was 32° C.). The solution was heated to 80° C and held for 5 minutes. The solution was diluted to 1000 L and cooled to 5° C. The solution was ultrafiltered until a final concentration of 20% solids was achieved and then spray diied. The molecular weight material greater than 30,000 Da was increased by 100% and the nunber of crossline s in the protein was 92 μmol/g.
- Extruded films were prepared using the following formulation on a Brabender Twin Screw extruder.
Ingredients Extrusion 1 Extrusion 2 Protein MAP112 (Example 3) 32.40 30.0 Milk derived calcium phosphate 32.40 30.0 Ace-K 0.99 1.0 Emulsifier 1.62 1.5 Flavour Peppermint Oil 6.48 6.0 Glycerol 16.20 13.0 Water 9.91 18.5 100.0 100.0
Method of Preparation - The liquid ingredients (water, glycerol, peppermint oil and emulsifier) were mixed and slowly added to the dry mix (Protein MAP112, Milk derived calcium phosphate and Acesulfame K) and stirred until all ingredients were well mixed. The pH was adjusted to 7.5 with 4M NaOH. The resulting mixture formed a thermoplastic mass that was crumbly at temperatures below 18° C. The mixture was cooled to 0° C. and ground to a powder.
- Extruder Conditions
- Feed hopper screw speed SRPM
- Extruder screw speed 8 RPM
- Barrel temperature profile (from feed end)
Section 1 50° C. Section 2 60° C. Section 3 65° C. Section 4 75° C. Nozzle 80° C. - Nozzle aperture 100 μm
- The crumble was fed into hopper and extruded as a thin film. As the film was exited the nozzle it was picked up by strips of paper (silicon backed, 0.25 μm thickness 2 m length). The paper speed was varied to achieve films with thicknesses ranging from 40 μm to 150 μm The films were packed in foil laminate bags.
- Determination of Degree of Cross Linking Using High Performance Liquid Chromatography
- Chemicals and Reagents
- ε-(γ-Glutamyl)lysine (G-L) and trifluoroacetic acid (TPA, protein sequencing grade), Prolidase (porcine, kidney), Leucine aminopeptidase and cytosol from hog kidney, Carboxypeptidase A (bovine pancreas) and Pronase (Streptomyces griseus) and TRIS [Tris(hydroxymethyl)aninomethane] were purchased from Sigma Chem Co. (Sydney, Australia). Acetonitrile (HPLC grade) was purchased from Biolab (Christchurch, New Zealand).
- Proteolytic Digestion of the Cross-Linked Proteins
- A 48-50 mg aliquot of protein sample was weighed in a glass test tube (total volume 15 mL). A crystal of thymol and 2 ml of 0.2 M Tris (H 8.0, HCl) was added, the solution vortexed and then incubated at 40° C. for 1 h to allow the dispersion of the protein. An aliquot of Pronase (0.4 U/mg protein) was added to the mixture which was then incubated at 37° C. for 24 h. The pronase digestion was continued for a fisher 24 h by the addition of another equal sized aliquot of pronase. After inactivation of pronase by heating at 100° C. (waterbath) for 10 min, the digestion was continued adding leucine aminopeptidase (0.4 U/mg protein), the solution being treated as for the pronase incubation. The digestion was continued using prolidase (0.45 U/mg protein) and then carboxypeptidase A (0.2 U/mg protein). After final inactivation the mixture was diluted to 7.5 g with ultrapure water (MilliQ water purification system)(Millipore, North Ryde, Australia).
- HPLC Analysis of GEL
- The HPLC system consisted of a Dionex GP40 gradient pump solvent delivery system connected to an ICI Instruments 1210 UV/Vis detector. Data was captured via an ITNS Acquisition Board and analysed using the AZUR chromatography software Version 1.1. The samples (100 μl) were separated on an Inertsil ODS-2 column (5 Em, 150×7.6 mm) (Phenomenex, Auckland, New Zealand) connected to a guard column (C18 ODS, 4 mm×3.0 mm ID)(Phenomenex) and a 2 Fun prefilter. Analysis was- performed at 2.5° C. The mobile phases were 0.1% TFA (v/v)(solvent A) and acetonitrile containing 0.1% TPA (v/v) (solvent B). Tfhe solvent program was as follows: 100% solvent A for 20 nn 0% to 100% solvent B from 20 to 25 min, 100% solvent B from 25 to 50 min. The detector wavelength was set at 210 nm and the flow rate was 1.0 ml/min.
- All samples from proteolytic digestion were filtered on a 0.45 Elm Millex-HA Millipore filter unit. 200 μl of sample was mixed with 100 μl of distilled water and 100μl TFA (2% w/w). The G-L peak was identified by comparison to elution time of a standard and confirmed by standard addition of a G-L standard solution to the sample.
-
5A 5B 5C Ingredients % weight/weight Phosphoprotein Lot2/18 22.5 — — MAP106 — 30 — MAP109 — — 30 Milk calcium phosphate 22.5 10 30 Ace-K 0.75 1 1 Emulsifier - Lamegin 609ZE 1.13 1.5 1.5 Flavor - Peppermint Oil B&J 4.5 6 6 Glycerol 7.5 18 15 Water 41.12 33.5 16.5
Method of Preparation: - The dry ingredients hosphoprotein, Alamin®, and Ace-K) were blended
- The characteristics of the phosphoproteins used in the preparations were as follows: Lot 102: degree of hydrolysis (DH) 8.8%, degree of cross linking IS0punol/g protein; MAP 106: DH 4.4%, degree of cross linking 155pmol/g protein, MAP 109: DH 5.7%, degree of cross linking 155 μmol/g protein.
- The liquid ingredients (emulsifier, flavor, glycerol and water) were blended, The mixture was heated gently to 30-40° C. as required, to dissolve the emulsifier.
- The dry ingredients were added slowly to the liquid ingredients, stirring until all ingredients were well mixed
- The pH was adjusted to 7.5 with 4M NaOH.
- The solution was spread onto a dry glass plate (0.25 mm thickness), and dried at 100-110° C. for about 4-5 minutes. The plate was left to rehydrate at room temperature and then the film peeled off the plate using a blade.
- Description of Films
- Lot2/18 and MAP106 made flexible, slightly sticky films that dissolved quickly. MAP109 was also very flexible, tasting slightly damp and clung briefly to the tongue before quickly dissolving. All films also gave an intense flavour burst.
-
6A 6B 6C 6D 6E Ingredients % weight/weight Phosphoprotein (MAP112) 30 27 27 22.5 23.1 Salts CaCl2 3 — — — — CaCO3 — 13.6 — — — Ca Citrate — — 13.6 — — Ca3PO4 — — — 27.1 — MgCl2 — — — — 23.1 Ace-K 1 0.9 0.9 0.8 0.8 Emulsifier - Lamegin 609ZE 1.5 1.4 1.4 1.1 1.2 Flavor - Peppermint 6 5.4 5.4 4.5 4.6 Glycerol 15 10.9 10.9 13.5 11.5 Water 43.5 40.8 40.8 24.9 35.8
Method of Preparation: - The films were prepared as per Example 6.
- Description of Films
- All the films were thin, flexible and dissolved quickly. All films also gave an intense flavour burst. The carbonate, citrate and phosphate films were opaque in colour, while the chloride films were clear. The films containing a chloride salt were slightly sticky.
- Method of Determining Degree of Hydrolysis of Partially Hydrolysed Casein
- Samples were prepared as either 0.1% or 1% protein (w/v) solutions in distilled water. A 100 μl aliquot of sample was added to 800 μl of 0.2125 M sodium phosphate buffer, pH 8.20. To this 800 pi 0.1% TNBS reagent was added, and the reagents were mixed well, wrapped in foil and incubated at 50° C. in a covered water-bath. After exactly 60 minutes the reaction was terminated by the addition of 1600 μl of 100 mM HCl and the samples left to cool to room temperature for 30 minutes before reading absorbance against a buffer/TNBS blank at 340 μm.
- As described above, the films of the present invention have a number of applications. For example, they may be used to deliver a breath freshener or other oral care agent Alternatively or additionally, they may act as a carrier for a pharmaceutical or veterinary agent, a nutraceutical agent, a salivay stimulant agent, a vitamin, a mineral or combinations thereof. In other applications, the edible films of the present invention may be used as a readily soluble and/or edible coating for foods such as fruit or confectionery products. They may also be used in food product labeling, such as cheese labeling. A further application is in the preparation of novel confections such as tongue tattoos.
- In still other applications, the films may be used to as a vehicle to apply active agents topically to the skin. For example, sunscreen (SPF) agents, burn recovery agents, Herpes simplex remedies, and topical antifungal disease agents may be incorporated in the films of the present invention.
- In still further applications, the films may be used in diagnostic kits, particularly in immunology, or in forensic applications.
- At least in the preferred embodiments, the edible films of the present invention have the advantage of “grabbing” less in the mouth and providing a relatively clean mouth feel on dissolution, as compared to certain currently available pullulan-based films. The quick getaway in the mouth of the films of the present invention also gives them potential for use in sudden flavor release.
- While the invention has been described in detail and with reference to particular embodiments thereof; various changes and modifications of these embodiments will be apparent to those skilled in the art. Such changes and modifications can be made without departing from the scope and scope of the present invention as defined in the appended claims.
Claims (33)
1. A film comprising:
(a) a phosphoprotein preparation, wherein the phosphoprotein preparation has been obtained by partially cross linking a partial hydrolysate of casein or a case mate;
(b) a source of one or more physiologically acceptable cations; and
(c) a plasticizer.
2. A film according to claim 1 , wherein the film is edible.
3. A film according to claim 1 , wherein the film is substantially soluble.
4. A film according to claim 1 , wherein the cations are divalent.
5. A film according to claim 1 , wherein the source of the cations comprises a substantially water-insoluble salt of the cations.
6. A film according to claim 1 any one of the preceding claims, wherein the cations comprise calcium ions.
7. A film according to claim 6 , wherein the source of calcium ions comprises calcium phosphate.
8. A film according to claim 7 , wherein some or all of the calcium phosphate is in the form of calcium hydroxyapatite.
9. A film according to claim 6 , wherein the source of calcium comprises natural milk calcium phosphate.
10. A film according to claim 9 , wherein the natural milk calcium phosphate and the phosphoprotein preparation are present in the film in a weight ratio of about 0.3:1 to about 1.3:1.
11. A film according to claim 1 , wherein the plasticizer comprises one or more polyhydric alcohols.
12. A film according to claim 11 , wherein the polyhydric alcohol comprises glycerol.
13. A film according to claim 1 , wherein the degree of hydrolysis of the casein or case mate prior to the partial cross linking is in the range of about 0.5% to about 10% of the total number of peptide bonds.
14. A film according to claim 13 , wherein the degree of hydrolysis of the casein or caseinate prior to the partial cross linking is in the range of about 2% to about 8% of the total number of peptide bonds.
15. A film according to claim 1 , wherein the partial hydrolysate of casein or a caseinate has been obtained by enzymatic hydrolysis of acid casein, rennet casein or a caseinate.
16. A film according to claim 15 , wherein the enzyme is trypsin, and the partial hydrolysis has been carried out at a pH of from about 7 to about 8.
17. A film according to claim 1 , wherein the partial cross linking has been carried out enzymatically, using transglutaminase.
18. A film according to claim 1 , wherein the degree of partial cross linking is such that the resulting phosphoprotein preparation comprises about 10 μmol or more cross links per gram of protein.
19. A film according to claim 18 , wherein the degree of partial cross linking is such that the resulting phosphoprotein preparation comprises between about 10 μmol and 250 μmol cross links per gram of protein.
20. A film according to claim 19 , wherein the degree of partial cross linking is such that the resulting phosphoprotein preparation comprises between about 50 μmol and 160 μmol cross links per gram of protein.
21. A film according to claim 1 , wherein the film further comprises one or more emulsifiers.
22. A film according to claim 21 , wherein the emulsifier comprises a citric acid ester of mono- and diglycerides.
23. A film according to claim 1 , wherein the film further comprises one or more additional agents selected from the group consisting of flavoring or breath freshening agents, sweeteners, coloring agents, pH control agents and stabilizers.
24. A film according to claim 1 , wherein the film further includes one or more active agents selected from the group consisting of an oral care agent, a pharmaceutical or veterinary agent, a nutraceutical agent, a salivary stimulant agent, a vitamin, a mineral and combinations thereof.
25. A food product including an edible coating comprising a film as claimed in claim 1 .
26. A process of producing an edible film, the process comprising
processing a mixture comprising (a) a phosphoprotein preparation, wherein the phosphoprotein preparation has been obtained by partially cross linking a partial hydrolysate of casein or a caseinate, (b) a source of one or more physiologically acceptable cations, and (c) a plasticizer, to form a film;
27. A process according to claim 26 , wherein the mixture includes water.
28. A process according to claim 26 , wherein the processing includes the steps of applying the mixture to a surface followed by drying to form the film.
29. A process according to claim 26 , wherein the processing comprises extruding the mixture to form a film.
30. A mixture capable of being processed to produce an edible film, the mixture comprising:
(a) a phosphoprotein preparation, wherein the phosphoprotein preparation has been obtained by partially cross linking a partial hydrolysate of casein or a caseinate;
(b) a source of one or more physiologically acceptable cations; and
(c) a plasticizer.
31. A mixture as claimed in claim 30 , wherein the mixture is thermoplastic and extrudable.
32. A mixture as claimed in claim 31 , which is in the form of a powder.
33. The process of claim 26 , additionally comprising drying the film to reduce the moisture content to a desired level.
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
NZ522071A NZ522071A (en) | 2002-10-18 | 2002-10-18 | Hydrolysed casein phosphoprotein preparations for bioactive metal ion delivery and teeth remineralisation |
NZ522071 | 2002-10-18 | ||
PCT/NZ2003/000231 WO2004035029A1 (en) | 2002-10-18 | 2003-10-20 | Edible phosphoprotein film |
Publications (1)
Publication Number | Publication Date |
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US20060225610A1 true US20060225610A1 (en) | 2006-10-12 |
Family
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Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US10/531,350 Abandoned US20060225610A1 (en) | 2002-10-18 | 2003-10-20 | Edible phosphoprotein film |
US10/531,435 Expired - Fee Related US7566742B2 (en) | 2002-10-18 | 2003-10-20 | Phosphoprotein preparations for bioactive metal ion delivery and teeth remineralisation |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
US10/531,435 Expired - Fee Related US7566742B2 (en) | 2002-10-18 | 2003-10-20 | Phosphoprotein preparations for bioactive metal ion delivery and teeth remineralisation |
Country Status (10)
Country | Link |
---|---|
US (2) | US20060225610A1 (en) |
EP (2) | EP1551377A4 (en) |
JP (2) | JP2006506981A (en) |
KR (1) | KR20050083775A (en) |
CN (2) | CN1729009A (en) |
AU (2) | AU2003278634A1 (en) |
BR (1) | BR0314880A (en) |
CA (1) | CA2502084A1 (en) |
NZ (1) | NZ522071A (en) |
WO (2) | WO2004035029A1 (en) |
Cited By (1)
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---|---|---|---|---|
CN110184029A (en) * | 2019-05-14 | 2019-08-30 | 山东省农业科学院农业质量标准与检测技术研究所 | A kind of peanut meal base albumen adhesive and its preparation method and application |
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US20030068375A1 (en) | 2001-08-06 | 2003-04-10 | Curtis Wright | Pharmaceutical formulation containing gelling agent |
WO2006007662A1 (en) * | 2004-07-22 | 2006-01-26 | Phoscal Holdings Pty Limited | Methods for increasing foam stability |
JP2008520565A (en) | 2004-11-16 | 2008-06-19 | スリーエム イノベイティブ プロパティズ カンパニー | Dental composition comprising calcium and phosphorus releasing glass |
AU2005306867B2 (en) | 2004-11-16 | 2011-09-08 | 3M Innovative Properties Company | Dental fillers and compositions including phosphate salts |
KR101366911B1 (en) | 2004-11-16 | 2014-02-24 | 쓰리엠 이노베이티브 프로퍼티즈 컴파니 | Dental fillers including a phosphorus-containing surface treatment, and compositions and methods thereof |
DE602005023509D1 (en) | 2004-11-16 | 2010-10-21 | 3M Innovative Properties Co | DENTAL FILLERS, METHOD, COMPOSITIONS USING A CASEINATE |
EP1827366B1 (en) | 2004-11-25 | 2017-03-15 | The University of Melbourne | Stabilized calcium phosphate complexes |
IL166114A0 (en) * | 2005-01-03 | 2006-01-15 | Calcident Active Ltd | Long-acting controlled-release pharmaceutical preparation for use in the oral cavity |
PT1888014E (en) | 2005-06-07 | 2013-02-15 | Univ Melbourne | Dental mineralization |
US8603988B2 (en) | 2005-06-24 | 2013-12-10 | The University Of Melbourne | Ionic complexes |
PL2705826T3 (en) | 2006-02-09 | 2020-11-02 | The University Of Melbourne | Fluoride composition and methods for dental mineralization |
EP2017191A4 (en) | 2006-05-10 | 2013-05-08 | Kureha Corp | Edible film package having product for oral intake enclosed therein |
KR101579946B1 (en) * | 2007-08-31 | 2015-12-28 | (주)디씨디 | Method and Kit for Isolating and Fractioning Phosphoproteins |
EP2185760B2 (en) * | 2007-08-31 | 2019-06-19 | Arçelik Anonim Sirketi | A washing machine |
GB0807224D0 (en) * | 2008-04-21 | 2008-05-28 | Univ Dundee | Remineralisation of calcified tissue |
GB0815051D0 (en) * | 2008-08-18 | 2008-09-24 | Univ Dundee | Apparatus and method for mineralising biological materials |
JP6006722B2 (en) * | 2010-08-24 | 2016-10-12 | セーフホワイト インコーポレイテッド | Methods and materials for giving teeth a white appearance |
ITNA20110016A1 (en) * | 2011-03-24 | 2012-09-25 | Francesco Addeo | PREPARATION OF A PRODUCT CONSISTING OF IMMOBILIZED PHOSPHOPEPTIDES ON HYDROXYAPATITIS FOR NUTRACEUTICAL AND (OTHER) INNOVATIVE AIMS |
WO2014000803A1 (en) * | 2012-06-28 | 2014-01-03 | Optimags Dr. Zimmermann Gmbh | Method for producing a film formulation for an edible film, and the use thereof |
CN103289418B (en) * | 2013-06-04 | 2015-07-29 | 太原理工大学 | A kind of preparation method of edible film |
CA2918441C (en) | 2013-07-23 | 2023-03-21 | The University Of Melbourne | A base and phosphopeptide stabilized amorphous calcium phosphate (acp) and/or amorphous calcium fluoride phosphate (acfp) for use in promoting remineralisation |
EP3086751B1 (en) | 2013-12-24 | 2023-07-12 | The University Of Melbourne | Stabilized stannous compositions |
WO2017074960A1 (en) * | 2015-10-26 | 2017-05-04 | Colgate-Palmolive Company | Oral care products and methods |
US10906950B2 (en) | 2016-08-19 | 2021-02-02 | The United States Of America As Represented By The Secretary Of Agriculture | Alkaline pH-modified edible casein-based films and coatings, and method for the making thereof |
MY197428A (en) | 2017-03-14 | 2023-06-16 | Univ Melbourne | Treatment for gingivitis |
KR101846511B1 (en) * | 2018-01-24 | 2018-04-06 | 충남대학교산학협력단 | Manufacturing method of functional food packaging films using hagfish skin gelatin and cinnamon-bark essential oil |
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2003
- 2003-10-20 AU AU2003278634A patent/AU2003278634A1/en not_active Abandoned
- 2003-10-20 AU AU2003278635A patent/AU2003278635B8/en not_active Ceased
- 2003-10-20 BR BR0314880-7A patent/BR0314880A/en not_active IP Right Cessation
- 2003-10-20 US US10/531,350 patent/US20060225610A1/en not_active Abandoned
- 2003-10-20 CN CNA2003801069305A patent/CN1729009A/en active Pending
- 2003-10-20 CN CNA2003801069273A patent/CN1728987A/en active Pending
- 2003-10-20 JP JP2004545096A patent/JP2006506981A/en active Pending
- 2003-10-20 WO PCT/NZ2003/000231 patent/WO2004035029A1/en not_active Application Discontinuation
- 2003-10-20 US US10/531,435 patent/US7566742B2/en not_active Expired - Fee Related
- 2003-10-20 EP EP03770169A patent/EP1551377A4/en not_active Withdrawn
- 2003-10-20 JP JP2004545097A patent/JP4723249B2/en not_active Expired - Fee Related
- 2003-10-20 CA CA002502084A patent/CA2502084A1/en not_active Abandoned
- 2003-10-20 KR KR1020057006651A patent/KR20050083775A/en not_active Application Discontinuation
- 2003-10-20 WO PCT/NZ2003/000232 patent/WO2004035077A1/en active Application Filing
- 2003-10-20 EP EP03770170A patent/EP1567184A4/en not_active Withdrawn
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US5543164A (en) * | 1994-06-17 | 1996-08-06 | The Regents Of The University Of California | Water-insoluble protein-based edible barrier coatings and films |
US6120592A (en) * | 1997-04-25 | 2000-09-19 | Brault; Denis | Biodegradable films containing caseinate and their method of manufacture by irradiation |
US20060073188A1 (en) * | 1999-03-31 | 2006-04-06 | Pierre Fabre Medicament | Fast-dissolving isotropic expanded microporous composition or structure for pharmaceutical, veterinary, dietetic, food or cosmetic use and method for obtaining same |
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Publication number | Priority date | Publication date | Assignee | Title |
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CN110184029A (en) * | 2019-05-14 | 2019-08-30 | 山东省农业科学院农业质量标准与检测技术研究所 | A kind of peanut meal base albumen adhesive and its preparation method and application |
Also Published As
Publication number | Publication date |
---|---|
NZ522071A (en) | 2005-07-29 |
CN1729009A (en) | 2006-02-01 |
BR0314880A (en) | 2005-08-02 |
JP2006506981A (en) | 2006-03-02 |
WO2004035029A1 (en) | 2004-04-29 |
KR20050083775A (en) | 2005-08-26 |
US20060135407A1 (en) | 2006-06-22 |
AU2003278635B8 (en) | 2010-04-22 |
EP1551377A1 (en) | 2005-07-13 |
EP1567184A4 (en) | 2006-06-21 |
EP1567184A1 (en) | 2005-08-31 |
JP2006512303A (en) | 2006-04-13 |
EP1551377A4 (en) | 2006-06-21 |
AU2003278635A1 (en) | 2004-05-04 |
JP4723249B2 (en) | 2011-07-13 |
US7566742B2 (en) | 2009-07-28 |
WO2004035077A1 (en) | 2004-04-29 |
CA2502084A1 (en) | 2004-04-29 |
CN1728987A (en) | 2006-02-01 |
AU2003278634A1 (en) | 2004-05-04 |
AU2003278635B2 (en) | 2009-11-05 |
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