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WO1989011227A1 - Inhibition du brunissement d'origine enzymatique - Google Patents

Inhibition du brunissement d'origine enzymatique Download PDF

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Publication number
WO1989011227A1
WO1989011227A1 PCT/US1989/002165 US8902165W WO8911227A1 WO 1989011227 A1 WO1989011227 A1 WO 1989011227A1 US 8902165 W US8902165 W US 8902165W WO 8911227 A1 WO8911227 A1 WO 8911227A1
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WO
WIPO (PCT)
Prior art keywords
protease
food
effective
kit
darkening
Prior art date
Application number
PCT/US1989/002165
Other languages
English (en)
Inventor
Petros S. Taoukis
Theodore P. Labuza
Shao-Wen Lin
Janet H. Lillemo
Original Assignee
Regents Of The University Of Minnesota
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Regents Of The University Of Minnesota filed Critical Regents Of The University Of Minnesota
Publication of WO1989011227A1 publication Critical patent/WO1989011227A1/fr

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Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/22—Cysteine endopeptidases (3.4.22)
    • C12Y304/22002—Papain (3.4.22.2)
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23B—PRESERVATION OF FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES; CHEMICAL RIPENING OF FRUIT OR VEGETABLES
    • A23B2/00—Preservation of foods or foodstuffs, in general
    • A23B2/70—Preservation of foods or foodstuffs, in general by treatment with chemicals
    • A23B2/725—Preservation of foods or foodstuffs, in general by treatment with chemicals in the form of liquids or solids
    • A23B2/729—Organic compounds; Microorganisms; Enzymes
    • A23B2/783—Microorganisms; Enzymes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23B—PRESERVATION OF FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES; CHEMICAL RIPENING OF FRUIT OR VEGETABLES
    • A23B4/00—Preservation of meat, sausages, fish or fish products
    • A23B4/14—Preserving with chemicals not covered by groups A23B4/02 or A23B4/12
    • A23B4/18—Preserving with chemicals not covered by groups A23B4/02 or A23B4/12 in the form of liquids or solids
    • A23B4/20—Organic compounds; Microorganisms; Enzymes
    • A23B4/22—Microorganisms; Enzymes; Antibiotics
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23B—PRESERVATION OF FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES; CHEMICAL RIPENING OF FRUIT OR VEGETABLES
    • A23B7/00—Preservation of fruit or vegetables; Chemical ripening of fruit or vegetables
    • A23B7/14—Preserving or ripening with chemicals not covered by group A23B7/08 or A23B7/10
    • A23B7/153—Preserving or ripening with chemicals not covered by group A23B7/08 or A23B7/10 in the form of liquids or solids
    • A23B7/154—Organic compounds; Microorganisms; Enzymes
    • A23B7/155—Microorganisms; Enzymes ; Antibiotics
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/22—Cysteine endopeptidases (3.4.22)
    • C12Y304/22003—Ficain (3.4.22.3)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/22—Cysteine endopeptidases (3.4.22)
    • C12Y304/22004—Bromelain (3.4.22.4)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/22—Cysteine endopeptidases (3.4.22)
    • C12Y304/22014—Actinidain (3.4.22.14)

Definitions

  • the subject invention relates to extending the shelf life of foods, and more specifically the use of proteolytic enzymes to inhibit oxidative darkening or browning of plant tissues, fruit tissues, or shellfish.
  • Enzymatic browning or oxidative darkening is a phenomenon which occurs in many types of foods. Such browning is desirable in certain types of foods such as apple juices, black tea, raisins, and dates. However, in a majority of fresh foods, such darkening is particularly objectionable to the consumer. Notable examples of foods subject to objectionable rapid browning include shrimp, lettuce, peaches, apples, and potatoes. Browning is most severe when the natural structure of the food is subjected to disorganization such as results from cutting, peeling, comminuting, pureeing, pitting, pulping, freezing, etc. Browning is generally accompanied by a change in other Organoleptic properties of the food product.
  • organoleptic properties are meant those properties of food capable of detection by human senses, especially appearance, and by other organoleptic properties is meant especially the taste and texture of the foods. Once such browning has occurred, the commercial value of the foods is dramatically diminished. Browning is also perceived by consumers to accompany a loss of nutritive value.
  • Ortho-diphenol derivatives also known as catechols
  • catechols are catalytically oxidized by polyphenol oxidase (PPO) (monophenol, dihydroxy phenylalanine: oxygen reductase, E.C.I.14.18.10).
  • PPO polyphenol oxidase
  • the products of the reaction are quinones. Quinones in turn polymerize to form dark, high molecular weight polymers. The molecular weight of the quinone polymers correlates with an increasingly brown product.
  • the polymerization reactions are non-enzymatic secondary reactions.
  • PPO is present in high concentrations in foods which are particularly sensitive to oxidative browning, for example mushrooms, potatoes, apples, bananas, tea leaves, coffee, and peaches.
  • preventing is meant a complete elimination of browning.
  • inhibition is meant any significant slowing of the rate of browning up to and including preventing of browning.
  • a variety of peach the Freestone
  • the variety has a better shelf life than traditional peach varieties.
  • the improved shelf life is compatible with a model in which the rate of quinone production is severely limited by low PPO concentration.
  • Blanching may be explained in terms of the model as effective because of thermal denaturation of PPO.
  • PPO is relatively heat stable enzyme.
  • apple four to five minutes at boiling temperatures are generally required to inactivate the enzyme.
  • blanching is relatively energy intensive, destructive of vitamins, and tends to alter the microstructural properties of the food product being treated.
  • Another method is altering the pH of the food product.
  • the effectiveness of pH alteration may be explained in terms of the model as effectively reducing enzyme activity, thereby inhibiting production of quinones.
  • Common agents employed to alter the pH are citric acid, malic acid, or phosphoric acid, or buffer solutions of these acids.
  • pH levels of about pH 3 are generally incompatible with maintenance of organoleptic properties, especially taste and texture, of many foods.
  • increasing the pH to approximately pH 8-9 through the use of phosphate buffers, also tends to alter the organoleptic properties of many foods.
  • chelating agents such as EDTA
  • reducing agents such as ascorbic acid and salts of ascorbic acid
  • Oxygen removal may be explained in terms of the model as eliminating the oxidant.
  • Another approach is to enzymatically alter the o-phenols by methylation. Success of enzymatic methylation is compatible with a model in which the substrate for PPO has been eliminated. (See Finkle, 197 Nature 902-903 (1963); U.S. Patent 3,126,287.) Substrate elimination may also be achieved by a ring-cleaving enzyme, such as protocatechuate 3,4 dioxygenase. See Kelly, 20 F. Fd. Agric. 629-32 (1969).
  • Sulfite salts have been used in the food and beverage industry for centuries. For example, sulfur dioxide was employed to disinfect wine vessels since
  • Sulfite salts are highly effective in controlling enzymatic browning of foods. Additionally, sulfite salts serve as bleaches, and antimicrobials. Based mainly on such a longstanding history of use, sulfites were considered safe additives for food. Recently, however, sulfite salts have been implicated as initiators of dangerous asthmatic reactions in a small subset of the asthmatic population, estimated at between 180,000-720,000 individuals in the United States.
  • a single 100 gram portion of lettuce treated with sulfite might include from 40-95 mg. of sulfite.
  • the present invention includes a process of inhibiting oxidative darkening of foods by treating of the food with a protease which is effective to inhibit oxidative darkening of the food.
  • the present invention also includes a kit comprising a soluble protease effective to prevent oxidative browning and a container for storing the soluble protease prior to use.
  • enzymatic oxidative darkening can be inhibited by treatment of a food with a protease.
  • treatment is meant contacting the food or a disorganized surface of the food with the protease or a solution of the protease by any application method including dusting, mixing, sprinkling, dipping, spraying, immersing or soaking, etc.
  • the mechanism while not yet proven, is believed to be hydrolysis and thereby permanent inactivation of the food enzymes, for example, PPO, responsible for oxidative darkening.
  • Some of the proteases effective to prevent oxidative darkening are well known in the food industry.
  • One effective protease, papain has been used as a meat tenderizer for many years. However, the use of papain or other proteases to inhibit or prevent oxidative browning has not been previously reported.
  • the invention includes the use of a protease to inhibit oxidative darkening.
  • enzymes is meant proteins which catalyze chemical reactions.
  • PPO is one example of an enzyme.
  • Proteases are a subgroup of enzymes which catalyze hydrolysis of proteins into peptides and/or amino acid residues. It is generally believed that hydrolysis of an enzyme will reduce or eliminate the catalytic activity of the enzyme.
  • an effective protease of the invention acts to hydrolyze and therefore inactivate the enzyme or enzymes responsible for enzymatic browning.
  • PPO polyphenol oxidase
  • inactivation of PPO prevents or inhibits the oxidation of O-diphenols to quinone compounds. Since quinones are the precursors of high molecular weight polymers responsible for darkening of foods, completely eliminating the enzyme activity of PPO is a highly effective method to prevent enzymatic oxidative browning.
  • any protease which will hydrolyze and thereby inactive PPO will inhibit the browning reaction.
  • the protease applied to the food be safe for subsequent human consumption.
  • enzymes commonly available for use in the food industry are particularly preferred.
  • One well known enzyme, papain is currently considered as "generally recognized as safe” (GRAS) by the FDA. (See 21 C.F.R. ⁇ 184.1585.)
  • GRAS generally recognized as safe
  • other proteases which may be isolated from common foods are believed useful.
  • Ficin, isolated from fig, and actinidin (E.C.3.4.22.14) isolated from kiwi fruit represent two examples.
  • Papain and ficin have been found to inhibit enzymatic browning of apples and potatoes, respectively. Ficin also inhibits or prevents black spot formation in shrimp. The results obtained are comparable to the inhibition of browning provided by sulfite treatment. Not all proteases, however, are capable of satisfactorily inhibiting browning. For instance, only when apple and potato are stored at 24 ⁇ C can bacterial protease exhibit satisfactory inhibitory results. Bromelain cannot inhibit the browning effect except in the case of an apple stored at 4 ⁇ C. Fungal protease appeared to accelerate the browning of apples stored at 24'C.
  • testing for the effectiveness of a particular protease requires treating a desired food of solid, puree or liquid form by exposure to the dry protease or a solution of the protease. Instrumental measurement or visual observation of the treated food in comparison to an untreated sample reveals the effectiveness of the particular protease. Similarly, amounts or concentrations of the protease necessary for effective inhibition may be determined by comparison to an untreated sample of the food.
  • the upper limit of useful concentrations or amounts of protease with which a food is treated is believed to be controlled primarily by the market price of the protease.
  • the lower limit is believed to be controlled by the economics of exposure times, since lower protease concentrations are generally believed to require longer exposure to be effective.
  • proteases used were obtained from Enzyme Development Corp., New York, NY 10121: specifically Enzeco Bromelain, Enzeco Neutral Bacterial Protease, Enzeco Purified Papain, Enzeco Ficin, and Enzeco Fungal Protease were used. All other chemicals used were AR grade.
  • the activities of the proteases used were approximately 100 Milk Clot Units per milligram for ficin, bromelain, and papain; 150 Northrup Units per gram for bacterial protease; and 100,000 H.U.T.
  • Hemoglobin Units per gram for fungal protease Hemoglobin Units per gram for fungal protease.
  • a series of 2 percent weight/volume enzyme solutions was prepared by mixing each enzyme with 125 ml 0.1 molar citric buffer (pH 4.5).
  • the citric buffer and 0.5 percent NaHS0 3 solution were used as controls.
  • Apples (Red Delicious) were cored and cut, under water (at about 10*C) into about 5 mm thick pieces of about 4 cm diameter, and soaked for about 5 minutes in the different solutions.
  • Duplicate samples for each treatment were put in Petri dishes and stored at 24 * or 4 ⁇ C in a desiccator saturated with water vapor so as to avoid surface dehydration of the samples. Untreated duplicate samples were stored similarly as a control.
  • the color changes of the samples were measured by Tristimulus reflectance colorimetry, using a Minolta Chroma eter CR-200, at the initial and subsequent time intervals.
  • Example 2 A procedure similar to Example 1 was employed to measure inhibition of browning in white baking potato slices.
  • the pH of the citric buffer was 5.2 rather than pH 4.5 as in Example 1.
  • Table II normalized L values of the potato samples were measured at various time intervals. Careful visual observation of potato slices indicated that, as with apple slices, a normalized L value of about 0.97 cannot be distinguished from the initial slice. Slight browning corresponds to a normalized L value of about 0.95 and is subjectively considered as the lowest acceptable result.
  • ficin is as effective or nearly as effective as sulfite treatment in inhibiting enzymatic browning of potatoes at room and refrigerated temperatures.
  • Bacterial protease was also effective at room temperature. Papain showed a limited effect. Bromelain and fungal protease were generally ineffective in inhibiting browning.
  • Example 3 The Inhibition of Black Spot Formation on Shrimp by Ficin.
  • De-headed fresh shrimp, Florida Key Pink were provided by the Singleton Seafood Company (Key West, FL 33040) and were certified to be free from any additives or chemical treatments by Singleton Seafood Company.
  • the shrimp were treated in the solutions as described in Example 1, except for the pH of the buffer, which was 5.2 for shrimp. Untreated shrimp were also included as a control.
  • the samples, in four replicates for each treatment, were put in Petri dishes and stored at 24°C, 4 ⁇ C, and under frozen condition (-25 ⁇ C). At the initial time and at subsequent desired time intervals, the samples were visually inspected for identification and enumeration of black spots. Subsequent to treatment, no new black spots were formed. Therefore, the ficin treatment effectively prevents black spot formation in shrimp. For example, the results of 4 ⁇ C storage presented in Table III demonstrate the effectiveness of ficin in preventing black spot formation.
  • the invention also includes a convenient kit for use in the food industry.
  • the kit includes a container with an effective soluble protease. Within the container, the protease is protected from moisture and other environmental conditions which reduce protease activity during storage. When a food worker desires to prevent oxidative darkening of solid foods, the worker opens the container and mixes the protease with water or buffer. For liquid food or purees, the protease can alternatively be added in a dry form.
  • the kit also includes instructions on preparing the protease solution. Direct application of powdered enzyme to foods is also effective. The instructions suggest the most appropriate concentration and warn against frothing during mixing. Additionally, the instructions include appropriate methods of application and duration of treatment time to achieve an effective treatment of the food. Effective application methods include dipping, misting, dusting, mixing or spraying or any other method in which the food is contacted by an effective amount of the protease for a time period effctive to inhibit darkening.
  • the kit may also include a suitable dry buffer composition.
  • a suitable dry buffer composition When mixed with water, preferably tap water, the dry buffer composition dissolves to provide a pH buffer compatible with the food to be treated and compatible with protease activity. Because time and efficiency of preparation are highly important in the food industry, the inclusion of a buffer composition requiring only addition to a measured quantity of water is desirable.
  • the buffer composition and protease are packaged together.
  • One problem with protease solutions is the tendency to self hydrolyze, thus often causing a rapid loss in activity. Therefore, the freshness of the solution is desirable in efficient use of the protease.
  • the kit of this invention is particularly suited to preparation of fresh protease solutions and freshness can be emphasized in the accompanying instructions.

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  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Organic Chemistry (AREA)
  • Wood Science & Technology (AREA)
  • Zoology (AREA)
  • Biochemistry (AREA)
  • Health & Medical Sciences (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Polymers & Plastics (AREA)
  • Food Science & Technology (AREA)
  • Microbiology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Food Preservation Except Freezing, Refrigeration, And Drying (AREA)
  • Storage Of Fruits Or Vegetables (AREA)

Abstract

Procédé servant à empêcher la coloration sombre des aliments provoquée par l'oxydation, consistant à traiter lesdits aliments avec une protéase qui inhibe efficacement le brunissement dû à l'oxydation. On décrit une préparation inhibant le brunissement dû à l'oxydation, ainsi qu'un kit permettant d'obtenir cette préparation.
PCT/US1989/002165 1988-05-20 1989-05-18 Inhibition du brunissement d'origine enzymatique WO1989011227A1 (fr)

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US197,038 1988-05-20

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Cited By (12)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5059438A (en) * 1990-02-05 1991-10-22 Enzytech, Inc. Compositions and methods for inhibiting browning in foods using resorcinol derivatives
WO1992013461A1 (fr) * 1991-01-30 1992-08-20 Pillsbury Co Traitement enzymatique de la totalite des fragments de membranes
US5202141A (en) * 1990-02-05 1993-04-13 Mcevily Arthur J Compositions and methods for inhibiting browning in foods and beverages
EP0599868A1 (fr) * 1991-07-17 1994-06-08 Commonwealth Scientific And Industrial Research Organisation Genes de polyphenol oxydase
WO1995032632A3 (fr) * 1994-05-26 1996-05-23 Richard G Rowland Traitements antimicrobien et conservateurs des produits frais d'origine vegetale
US6627794B1 (en) 1995-05-23 2003-09-30 Commonwealth Scientific And Industrial Research Organisation Polyphenyl oxidase genes from banana
WO2006023997A3 (fr) * 2004-08-23 2006-09-21 Micro Tender Ind Composition et procede d'attendrissement de viande
EP1906744A2 (fr) * 2005-07-01 2008-04-09 Advanced Biochemicals Limited Brunissage commande au moyen d'un exhausteur biologique
US7381810B2 (en) 1995-05-23 2008-06-03 Commonwealth Scientific And Industrial Research Organistion Polyphenol oxidase genes from lettuce
US8163317B2 (en) 2000-11-17 2012-04-24 Danisco A/S Method
CN112868749A (zh) * 2021-03-04 2021-06-01 天津市农业科学院 一种延长鲜切马铃薯保鲜期的方法及应用
CN116076649A (zh) * 2022-11-08 2023-05-09 广东佳宝集团有限公司 一种果品原料灭活酶的加工方法及抑制色素褐变处理设备

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US2474650A (en) * 1944-06-21 1949-06-28 Dehydration Inc Treatment of vegetable tissue
US3469995A (en) * 1965-12-23 1969-09-30 Adolph Food Prod Mfg Co Meat additives
US4207344A (en) * 1975-06-14 1980-06-10 Cerrillo Vincente P Processes for protecting proteic foodstuffs against spoilage
US4419370A (en) * 1980-02-25 1983-12-06 B. C. Research Council Fish canning process
JPS5963132A (ja) * 1982-09-30 1984-04-10 Toyobo Co Ltd 魚介類の冷凍保存法

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US2474650A (en) * 1944-06-21 1949-06-28 Dehydration Inc Treatment of vegetable tissue
US3469995A (en) * 1965-12-23 1969-09-30 Adolph Food Prod Mfg Co Meat additives
US4207344A (en) * 1975-06-14 1980-06-10 Cerrillo Vincente P Processes for protecting proteic foodstuffs against spoilage
US4419370A (en) * 1980-02-25 1983-12-06 B. C. Research Council Fish canning process
JPS5963132A (ja) * 1982-09-30 1984-04-10 Toyobo Co Ltd 魚介類の冷凍保存法

Non-Patent Citations (2)

* Cited by examiner, † Cited by third party
Title
Derwent File Supplier WPI(L) AN - 82-33898E, 1982 Derwent Publ. (London, GB) & JP-A-5704766 (ASAHI DENKA KOGYO) 18 March 1982 *
Derwent File Supplier WPI(L) AN - 84-124979, 1984 Derwent Publ. (London, GB) & JP-A-59063132 (TOYOBO K.K.) 10 April 1984 *

Cited By (20)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5202141A (en) * 1990-02-05 1993-04-13 Mcevily Arthur J Compositions and methods for inhibiting browning in foods and beverages
US5304679A (en) * 1990-02-05 1994-04-19 Opta Food Ingredients, Inc. Compositions and methods for inhibiting browning in foods
US5059438A (en) * 1990-02-05 1991-10-22 Enzytech, Inc. Compositions and methods for inhibiting browning in foods using resorcinol derivatives
WO1992013461A1 (fr) * 1991-01-30 1992-08-20 Pillsbury Co Traitement enzymatique de la totalite des fragments de membranes
EP0599868A1 (fr) * 1991-07-17 1994-06-08 Commonwealth Scientific And Industrial Research Organisation Genes de polyphenol oxydase
EP0599868A4 (fr) * 1991-07-17 1995-03-29 Commw Scient Ind Res Org Genes de polyphenol oxydase.
US6703542B1 (en) 1991-07-17 2004-03-09 Commonwealth Scientific And Industrial Research Organisation Polyphenol oxidase genes
US6936748B1 (en) 1991-07-17 2005-08-30 Commonwealth Scientific And Industrial Research Organisation Polyphenol oxidase genes from potato tuber, grape, apple and broad bean
WO1995032632A3 (fr) * 1994-05-26 1996-05-23 Richard G Rowland Traitements antimicrobien et conservateurs des produits frais d'origine vegetale
US7381810B2 (en) 1995-05-23 2008-06-03 Commonwealth Scientific And Industrial Research Organistion Polyphenol oxidase genes from lettuce
US6627794B1 (en) 1995-05-23 2003-09-30 Commonwealth Scientific And Industrial Research Organisation Polyphenyl oxidase genes from banana
US8163317B2 (en) 2000-11-17 2012-04-24 Danisco A/S Method
US8956670B2 (en) 2000-11-17 2015-02-17 DuPont Nutrition BioScience ApS Method for the control of the formation of acrylamide in a foodstuff
US7250184B2 (en) * 2004-08-23 2007-07-31 Micro-Tender Industries Composition and method for tenderizing meat
WO2006023997A3 (fr) * 2004-08-23 2006-09-21 Micro Tender Ind Composition et procede d'attendrissement de viande
EP1906744A2 (fr) * 2005-07-01 2008-04-09 Advanced Biochemicals Limited Brunissage commande au moyen d'un exhausteur biologique
EP1906744A4 (fr) * 2005-07-01 2011-05-18 Advanced Enzyme Technologies Ltd Brunissage commande au moyen d'un exhausteur biologique
CN112868749A (zh) * 2021-03-04 2021-06-01 天津市农业科学院 一种延长鲜切马铃薯保鲜期的方法及应用
CN112868749B (zh) * 2021-03-04 2022-12-30 天津市农业科学院 一种延长鲜切马铃薯保鲜期的方法及应用
CN116076649A (zh) * 2022-11-08 2023-05-09 广东佳宝集团有限公司 一种果品原料灭活酶的加工方法及抑制色素褐变处理设备

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