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WO1999058309A1 - Traitement du liege avec une enzyme d'oxydation de phenol - Google Patents

Traitement du liege avec une enzyme d'oxydation de phenol Download PDF

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Publication number
WO1999058309A1
WO1999058309A1 PCT/DK1999/000226 DK9900226W WO9958309A1 WO 1999058309 A1 WO1999058309 A1 WO 1999058309A1 DK 9900226 W DK9900226 W DK 9900226W WO 9958309 A1 WO9958309 A1 WO 9958309A1
Authority
WO
WIPO (PCT)
Prior art keywords
cork
enzyme
phenol oxidising
treatment
stoppers
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.)
Ceased
Application number
PCT/DK1999/000226
Other languages
English (en)
Inventor
Lars Sparre Conrad
Wolf-Rüdiger SPONHOLZ
Otto Berker
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Novo Nordisk AS
Original Assignee
Novo Nordisk AS
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 Novo Nordisk AS filed Critical Novo Nordisk AS
Priority to ES99914448T priority Critical patent/ES2203104T3/es
Priority to AU33272/99A priority patent/AU753129B2/en
Priority to EP99914448A priority patent/EP1077796B1/fr
Priority to AT99914448T priority patent/ATE244116T1/de
Priority to DE69909286T priority patent/DE69909286D1/de
Priority to NZ508070A priority patent/NZ508070A/en
Publication of WO1999058309A1 publication Critical patent/WO1999058309A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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Classifications

    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B27—WORKING OR PRESERVING WOOD OR SIMILAR MATERIAL; NAILING OR STAPLING MACHINES IN GENERAL
    • B27K—PROCESSES, APPARATUS OR SELECTION OF SUBSTANCES FOR IMPREGNATING, STAINING, DYEING, BLEACHING OF WOOD OR SIMILAR MATERIALS, OR TREATING OF WOOD OR SIMILAR MATERIALS WITH PERMEANT LIQUIDS, NOT OTHERWISE PROVIDED FOR; CHEMICAL OR PHYSICAL TREATMENT OF CORK, CANE, REED, STRAW OR SIMILAR MATERIALS
    • B27K5/00—Treating of wood not provided for in groups B27K1/00, B27K3/00
    • B27K5/04—Combined bleaching or impregnating and drying of wood
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B27—WORKING OR PRESERVING WOOD OR SIMILAR MATERIAL; NAILING OR STAPLING MACHINES IN GENERAL
    • B27K—PROCESSES, APPARATUS OR SELECTION OF SUBSTANCES FOR IMPREGNATING, STAINING, DYEING, BLEACHING OF WOOD OR SIMILAR MATERIALS, OR TREATING OF WOOD OR SIMILAR MATERIALS WITH PERMEANT LIQUIDS, NOT OTHERWISE PROVIDED FOR; CHEMICAL OR PHYSICAL TREATMENT OF CORK, CANE, REED, STRAW OR SIMILAR MATERIALS
    • B27K3/00—Impregnating wood, e.g. impregnation pretreatment, for example puncturing; Wood impregnation aids not directly involved in the impregnation process
    • B27K3/002—Impregnating wood, e.g. impregnation pretreatment, for example puncturing; Wood impregnation aids not directly involved in the impregnation process employing compositions comprising microorganisms
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B27—WORKING OR PRESERVING WOOD OR SIMILAR MATERIAL; NAILING OR STAPLING MACHINES IN GENERAL
    • B27K—PROCESSES, APPARATUS OR SELECTION OF SUBSTANCES FOR IMPREGNATING, STAINING, DYEING, BLEACHING OF WOOD OR SIMILAR MATERIALS, OR TREATING OF WOOD OR SIMILAR MATERIALS WITH PERMEANT LIQUIDS, NOT OTHERWISE PROVIDED FOR; CHEMICAL OR PHYSICAL TREATMENT OF CORK, CANE, REED, STRAW OR SIMILAR MATERIALS
    • B27K7/00—Chemical or physical treatment of cork
    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B67—OPENING, CLOSING OR CLEANING BOTTLES, JARS OR SIMILAR CONTAINERS; LIQUID HANDLING
    • B67B—APPLYING CLOSURE MEMBERS TO BOTTLES JARS, OR SIMILAR CONTAINERS; OPENING CLOSED CONTAINERS
    • B67B1/00—Closing bottles, jars or similar containers by applying stoppers
    • B67B1/03—Pretreatment of stoppers, e.g. cleaning, steaming, heating, impregnating or coating; Applying resilient rings to stoppers

Definitions

  • This invention relates to a process for preparing or treating cork or cork articles such as cork stoppers.
  • Cork stoppers are used in various closures for perfumed compositions and alcoholic beverages such as wine, champagne and beer.
  • Cork is bark from the cork oak, e.g. Quercus suber L, which grows predominately in countries near the Mediterranean
  • cork stoppers commences with the stripping of the reproduction bark from the tree to provide cork slabs. These slabs are stored for up to two years. Usually, the slabs are then graded and often bundled, boiled in water and stacked once more. Abundant mould growth may occur during storage .
  • Natural cork stoppers are inter alia used as closures for wine bottles. Such stoppers are cut or punched generally in the cork slab longitudinal plane.
  • Natural cork slices or disks are used inter alia in the production of laminate cork stoppers typically used as closures for champagne bottles. Still further, cork slices are used for 2 sealing purposes at the inner bottom of various screw caps.
  • Slices are usually cut perpendicular to the longitudinal direction of the cork slab.
  • the slab material can be used for natural cork stoppers or slices.
  • the remaining material viz. cork pieces or crumbs of varying size, is generally used for preparing granulate cork.
  • Very small cork particles can be used directly in the heating system of the factory as an energy source .
  • Granulate cork can be used for various purposes, among other things in the production of agglomerated stoppers. To this end the crumbs are ground, cleaned and classified into various particle ranges. Binders, and if desired other additives such as plasticizers and cutting aids, are mixed with the granulated cork of the desired particle size, and the composition is moulded or extruded into shape. Optionally, the thus formed product is then polished.
  • Laminate cork stoppers are usually used for large stoppers such as champagne bottles. Such stoppers comprise a stopper body and one or more slices or disks of natural cork at the lowermost body part.
  • the body part is typically made of agglomerated cork.
  • the different portions are typically glued together.
  • Liqueur or liquor stoppers usually comprise a cork body part, be it natural or agglomerated, and a top part.
  • the top part is typically made from plastic, wood or cork. The two portions are glued together.
  • the manufacturing process of cork slices or cork stoppers usually includes a step of bleaching the cork.
  • the traditional bleaching process uses hypochlorite, usually calcium hypochlorite. Oxalate is then used as a reductant. The precipitation of calcium oxalate endows 3 the stoppers with an appealing white appearance.
  • hydrogen peroxide is used, with citric acid or the enzyme catalase for the subsequent degradation of residual hydrogen peroxide . This bleaching is for the purpose of cosmetic appearance and desinfection.
  • the water content of the cork articles is adjusted to the desired level, usually 5-8%. This is for the purpose of ensuring the microbial stability of the stoppers.
  • the stoppers are dried in a stream of warm air, and then packaged.
  • Cork is a highly desirable stopper material, inter alia due to its excellent gasketing characteristics and its high resistance to water, most organic liquids and all but strong acid and alkali solutions.
  • Cork taint is an off-flavour (taste or odour foreign to the product) , frequently described as musty, mouldy or earthy.
  • Astringency, bitterness and tannic flavour are specific variants of cork off- flavour .
  • cork taint in particular the astringency and/or bitterness and/or tannic flavour, imparted to food or perfumed products in contact with cork.
  • this object is achieved by treating or impregnating cork or cork articles with a phenol oxidising enzyme. 4
  • the invention relates to a process for preparing cork articles which comprises the step of treating cork with a phenol oxidising enzyme.
  • the invention also relates to a process for the treatment of cork, which comprises the step mentioned above.
  • the invention relates to the use of a phenol oxidising enzyme in the preparation or treatment of cork or cork articles.
  • the invention relates to a cork article (or cork) obtainable, in particular obtained, by any of the processes described herein.
  • the invention in a fourth aspect, relates to a cork article (or cork) which is characterized by an increased water repellency, as compared to a relevant control article which has been treated or prepared exactly as the article in question, except for the treatment with a phenol oxidising enzyme.
  • the test below is a preferred test for water repellency.
  • a preferred relevant control article is of the same batch and the same quality as the article in question.
  • the invention also relates to objects, preferably packaging objects, such as containers, boxes, cases, casks, glasses, bottles and the like, which objects are closed, sealed or stopped using a cork or a cork article of the invention.
  • Preferred objects are bottles.
  • Preferred bottles contain red or white wine, champagne, liquor, beer, lemonade, juice and the like; or perfumes; or other liquid compositions.
  • Water repellency can be detected or traced by a wetting analysis using the Lif-shitz-van der Waal / Lewis acid-base 5 approach (van Oss C.J., M. K. Chaudhury and R.J.Good, 1987; Monopolar Surfaces; Advances in Colloid and Interface Science, 28, 35-64; hereby incorporated by reference).
  • the Lewis base component and thereby the ability of the surface layer to donate electrons is drastically reduced by an oxidative treatment of the invention. Contrary, the Lewis acid component is not or only very little affected by such treatment.
  • An oxidation using other oxidizing agents, e.g. hydrogen peroxide will show a different Lewis acid/base pattern.
  • treatment of cork or cork articles such as stoppers with a phenol oxidising enzyme will also have a sterilising effect (the combination of certain phenols with a phenol oxidising system is known to have an anti-microbial effect) . It is also conceivable that by treating cork slabs with a phenol oxidising enzyme the storage time can be reduced.
  • the treatment of the invention improves the uniformity of a batch of wine, probably by eliminating or reducing the impact from cork stoppers of varying quality on the flavour or taste of such batch (see Example 3) .
  • the invention sets a new and improved standard for uniformity of flavour or taste, in particular for wine and the like alcoholic beverages.
  • An oxidation is an electron transfer reaction between two reactants: A donor looses an electron, an acceptor gains the electron; one of the reactants is oxidised (the electron donor) , the other reactant is reduced (the acceptor) .
  • Enzymes catalysing such reactions are called oxidoreductases .
  • Phenol oxidising enzyme In the present context the concept of a "phenol oxidising enzyme” includes any oxidoreductase acting on phenols and 6 related substances as donors with oxygen or hydrogen peroxide as acceptor, as well as enzymes which are positive in the test of Example 1 herein. This definition includes enzymes derived from animals, plants and microorganisms, as well as mutants and variants thereof which retain their phenol oxidising enzymatic activity.
  • this concept of a "phenol oxidising enzyme” includes whatever compounds necessary for the actual enzyme to work, i.e. for instance an appropriate acceptor. Such acceptor may or may not be naturally present in the reaction system.
  • phenol oxidising enzyme system a phenol oxidising enzyme system
  • Other components such as activators etc. are included in the concept of a "phenol oxidising enzyme system” to the extent such components are desirable for the enzyme to work optimally under the actual conditions. This optimization of the enzyme catalyzed reaction is a matter of routine for the skilled man, once a specific enzyme has been selected.
  • phenols means any compound which comprises at least one phenolic ring structure, i.e. an aromatic ring structure, in particular a benzene ring structure, with at least one OH-substituent at a ring C-atom, whatever other substituents, and whatever the number of condensed benzene rings.
  • This definition in particular comprises (mono) phenols, as well as polyphenols, such as di-, tri-, tetra-, penta- and hexaphenols.
  • tannins see e.g. Grant &hackh' s Chemical Dictionary, 5 th edition, McGraw-Hill Book Company, 1987, p. 574 in particular, hereby incorporated by reference
  • Guaiacol (2-methoxyphenol) is one example of a phenol detected in tainted wine and its associated cork.
  • the guaiacol taint is described as smokey, phenolic or medicinal.
  • Several other phenols are contemplated to contribute to the overall off- flavor.
  • composition of a cork material depends on its growth conditions, however a typical natural cork contains around 16 weight% lignin and 4 weight% tannins and miscellaneous organics, such as resorcinol, hydroquinone, salicylic acid, phloroglucinol and sterols.
  • phenols of potential relevance to cork taint are pentachlorophenol, 2, 3, 4 , 6-tetrachlorophenol, 3,4,5- trichlorophenol, 2, 4 , 6-trichlorophenol; dichlorocresols, such as derivatives of o-cresol, m-cresol and p-cresol.
  • dichlorocresols such as derivatives of o-cresol, m-cresol and p-cresol.
  • Another phenolic compound believed to be a major contributor to cork off-flavour is TCA (2, , 6-trichloro anisole) (Wine - microbiology and biotechnology, Graham H. Fleet (Ed.), Harwood Academic Publishers, 1993, pp.359-360).
  • Anisoles are probably formed in the cork by microbial transformation of phenols.
  • cork and cork articles The concept of "cork” as used herein includes bark from trees, in particular from cork oaks, whatever the physical form thereof, be it slabs, larger or minor parts thereof, such as cut-out stoppers and slices, as well as crumbs or compositions comprising crumbs, e.g. granulate cork. Also any more or less 8 worked up cork intermediate products (on the way to cork articles) are included in the definition of cork.
  • the expression “cork” is also intended to cover the expression “cork articles . " In the present context, a “cork article” is an article which contains cork. In other words: A cork article is the result of performing one or more process steps for which cork is used as a raw material.
  • a typical cork article is an article of commerce.
  • Preferred cork articles or products are cork closures or cork closure components, e.g. cork stoppers, cork slices or cork disks.
  • Other preferred cork articles are granulate or agglomerated cork articles.
  • Preferred cork stoppers are natural cork stoppers, laminate cork stoppers and agglomerated cork stoppers .
  • the treatment or impregnation of cork with a phenol oxidising enzyme can be performed in various ways. Basically, a composition comprising such enzyme (the enzyme preparation, be it liquid or dry) is applied to or brought into contact with cork.
  • the enzyme preparation is preferably liquid.
  • Preferred methods of treating or impregnating cork with liquid enzyme preparations are by dipping, spraying, immersing, injecting.
  • the interaction between the enzyme and the cork material may be enhanced, and the enzymatic effect on the cork material thus improved, by any means which improve the contact between enzyme and cork and/or the access of the enzyme to cork surface areas.
  • enzyme access to the so-called lenticels of the cork (the brown "eyes") is believed to be advantageous.
  • contact-improving means Means which minimize the water repelling effect of the cork surface, 9 e.g. surface tension lowering compounds and compositions; solvents; mechanical means such as ultrasonic treatment, aeration, stirring, vacuum, overpressure.
  • suitable solvents preferably an alcohol such as ethanol, is added to the enzyme containing treatment liquid.
  • the enzyme treatment takes place in a liquid comprising water and ethanol.
  • a preferred amount of ethanol is in the range of 1-30%, preferably 2-25%, more preferably 3-20%, even more preferably 5-15% (all percentages in vol/vol) .
  • the treatment takes place in an ultrasonic bath.
  • the ultrasonic treatment is combined with using a liquid which comprises alcohol.
  • the step of treating cork with a phenol oxidising enzyme can be performed at any step in the preparation of cork articles.
  • the impregnation should take place following the cutting of the cork slabs.
  • impregnation of already finalized cork articles is a preferred option.
  • repeated steps of impregnating with a phenol oxidising enzyme can be performed over the whole life time of the cork article.
  • a typical process for preparing cork stoppers ends up with a bleaching step and a final drying step. Optionally, a further desinfection step is included.
  • the treatment of the invention is performed following the bleaching step, in particular following the drying step or the desinfection step, whatever the later.
  • the treatment of the invention is performed following the bleaching step, in particular following the drying step or the desinfection step, whatever the later.
  • the treatment of the invention is performed before the bleaching step.
  • the phenol oxidising enzyme is a phenolic oxidase or a peroxidase.
  • Preferred phenolic oxidases are enzymes of classes EC 1.13.-.-; EC 1.14.-.- and EC 1.10.3.-, in particular any of the classes EC 1.10.3.1-1.10.3.8, and preferred peroxidases are enzymes of class EC 1.11.1.7 (Enzyme Nomenclature, 1992, Published for the International Union of Biochemistry and Molecular Biology (IUBMB) by Academic Press, Inc.; 1992).
  • the group EC 1.11.1.7 comprises peroxidases, catalysing oxidation reactions in which a donor is oxidised, hydrogenperoxide acting as the acceptor.
  • the grouping EC 1.10.3.- comprises enzymes acting on diphenols and related substances as donors with oxygen as acceptor.
  • Preferred enzymes of these classes are: Catechol oxidases (EC 1.10.3.1); laccases (alternative name urishiol oxidases, EC 1.10.3.2); and o-aminophenol oxidases (EC 1.10.3.4).
  • Monophenols however, are also very good substrates.
  • the grouping EC 1.14.18.1 comprises monophenol monooxygenase (alternative name tyrosinase, phenolase, monophenol oxidase, cresolase) .
  • the phenol oxidising enzymes are preferably purified, viz. only minor amounts of other proteins being present.
  • the expression "other proteins" relate in particular to other 11 enzymes.
  • the enzymes are at least 75% (w/w) pure, more preferably at least 80, 85, 90 or even at least 95% pure.
  • the phenol oxidising enzyme is at least 98% pure enzyme protein.
  • Preferred phenol oxidising enzymes are listed below. Any enzymatically active variants or mutants thereof are also preferred phenol oxidising enzymes. The activities thereof can be measured by any method known in the art.
  • Suitable peroxidases may be any peroxidase enzyme comprised by the enzyme classification (EC 1.11.1.7), or any fragment derived therefrom, exhibiting peroxidase activity.
  • the peroxidase is derived from plants (e.g. horseradish or soybean peroxidase) or microorganisms such as fungi or bacteria.
  • Some preferred fungi include strains belonging to the subdivision Deuteromycotina, class Hypho- mycetes, e.g., Fusarium, Humicola, Trichoderma, Myrothecium, Verticillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia, Cladosporium or Dreschlera, in particular Fusarium oxysporum (DSM 2672), Humicola insolens, Trichoderma resii, Myrothecium verrucana (IFO 6113), Verticillium alboatrum, Verticillum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago, Ulocladium chartarum, Embellisia alii or Dreschlera halodes .
  • DSM 2672 Fusarium oxysporum
  • Humicola insolens Trichoderma resii
  • Myrothecium verrucana IFO
  • fungi include strains belonging to the sub-division Basidiomycotina, class Basidiomycetes, e.g. Coprinus, Phanerochaete, Coriolus or Trametes, in particular Coprinus cinereus f. microsporus (IFO 8371), Coprinus macrorhizus, Phanerochaete chrysosporium (e.g. NA-12) or Trametes (previously called Polyporus) , e.g. T. versicolor (e.g. PR4 28-A) . 12
  • fungi include strains belonging to the sub-division Zygomycotina, class Mycoraceae, e.g. Rhizopus or Mucor, in particular Mucor hiemalis.
  • Some preferred bacteria include strains of the order Actino-mycetales, e.g., Streptomyces spheroides (ATTC 23965), Strep-tomyces thermoviolaceus (IFO 12382) or Streptoverticillum verticillium ssp. verticillium.
  • Actino-mycetales e.g., Streptomyces spheroides (ATTC 23965), Strep-tomyces thermoviolaceus (IFO 12382) or Streptoverticillum verticillium ssp. verticillium.
  • Bacillus pumilus ATCC 12905
  • Bacillus stearothermophilus Rhodobacter sphaeroides
  • Rhodomonas palustri Rhodomonas palustri
  • Streptococcus lactis Pseudomonas purrocinia
  • Pseudomonas fluorescens NRRL B-ll.
  • bacteria include strains belonging to Myxococcus, e.g., M. virescens.
  • a recombinantly produced peroxidase is preferred, e.g., a peroxidase derived from a Coprinus sp., in particular C. macrorhizus or C. cinereus according to WO
  • Laccase enzymes of microbial and plant origin are well known.
  • a suitable microbial laccase enzyme may be derived from bacteria or fungi (including filamentous fungi and yeasts) and suitable examples include a laccase derivable from a strain of
  • Neurospora e.g., N. crassa, Podospora, Botrytis,
  • Collybia Fomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinus, e.g.
  • thermophila Scytalidium, Polyporus, e.g., P. pinsitus
  • Phlebia e.g., P. radita (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2-238885) , in particular laccases obtainable from Trametes, Myceliophthora, Scytalidium or Polyporus. 13
  • a suitable catechol oxidase may be derived from Solanum melongena (Phytochemistry, 1980, 19(8), 1597-1600) or from tea (Phytochemistry, 1973, 12(8), 1947-1955). Polyphenol oxidase may be derived from molds (Hakko Kogaku Zasshi, 1970, 48(3), 154- 160) . A mammalian monophenol monooxygenase (tyrosinase) has been described (Methods Enzymol., 1987, 142, 154-165). Other suitable monophenol monooxygenases can be derived from tea leaves (Prikl. Biokhim. Mikrobiol., 1997, 33(1), 53-56), from Chlorella (Ukr. Bot. Zh., 1986, 43(5), 56-59) or from Neurospora crassa (Methods Enzymol., 1987, 142, 165-169).
  • a generally preferred pH of the treatment liquid is pH 3- 10, preferably 3.5-9, more preferably 4-8, still more preferably 4-7.
  • a generally preferred temperature in the treatment step of the invention is 10-80°C, preferably 10-70°C, more preferably 15-60°C, still more preferably 20-50°C, most preferably 20-40°C.
  • a generally preferred treatment time is 5 minutes to 5 hours, preferably 5 minutes to 4 hours, more preferably 15 minutes to 3 hours, still more preferably ⁇ to 2 hours.
  • the concentration of oxygen as acceptor (relevant to the use of phenolic oxidases only, viz. e.g. laccase) is not critical. At 25°C and in normal atmosphere, water has an equilibrium concentration of oxygen of around 200 ⁇ M which is usually fully sufficient for the enzyme reactions to occur in a satisfactory way. If desired, however, of course the oxygen 14 concentration of the impregnation liquid could be increased, e.g. to saturation.
  • the concentration of hydrogenperoxide as acceptor is generally not critical. However, the selected peroxidase enzyme could be sensible to hydrogenperoxide (loose activity) .
  • concentration range of hydrogenperoxide is 0.010-lOmM, more preferably 0.020-8mM, still more preferably 0.05-5mM, even more preferably 0.100-2.5mM.
  • a preferred dosage of the phenol oxidising enzyme is 0.001-1000 mg enzyme protein per liter treatment liquid, preferably 0.01-100 mg, more preferably 0.1-20 mg/liter.
  • the amount of enzyme protein can be measured using any method known in the art. These dosage values are preferably based on purified enzyme protein, purified being defined as indicated above .
  • Cork slices for champagne cork stoppers are treated with a phenol oxidising enzyme as described below.
  • the amount of phenols extracted from the cork slices after the treatment is measured and compared to a control.
  • the cork slices treated with a phenol oxidising enzyme show a reduced level of extracted phenols .
  • Phenol oxidising enzyme A laccase enzyme derived from Myceliophthora thermophila (prepared as described in 15
  • Treatment liquid pH 7, room temperature.
  • Ten slices are transferred to 200 ml impregnation liquid and kept in contact with the liquid for 30 minutes under stirring.
  • Test for water-extractability of phenols The content of phenols in the thus boiled, fresh water is assayed using a Folins reagent which imparts a blue color proportional to the amount of phenolic compounds extracted.
  • Folins reagent is i.a. described in J. Biol. Chem. 73, 1927, p. 627-650, authors: Folin, 0. and Ciocalteau, V. C. (hereby incorporated by reference) .
  • gallic acid is preferably used as a reference standard. It should be noted, however, that only informative relative values are required for the present purpose.
  • This assay can be used to test whether a given enzyme can be expected to reduce the cork off-flavour, viz. whether it falls under the definition herein of a phenol oxidising enzyme. This can be expected if a reduced absorbancy results, as compared to the control, for at least one of the cork qualities. Such enzymes are called "positive" in this assay.
  • the assay conditions should reflect the characteristics of the selected enzyme to test (in particular its pH and temperature characteristics) . It lies within the routine capability of the skilled person to elect such conditions or to set up suitable simple experiments to establish such optimum conditions. For instance the above assay can be tried at three to four different pH values, preferably in the interval of pH 4-10, and at three to four different temperatures, e.g. ranging from 10 to 80°C. 17
  • Quality grade 1 is the higher quality, 3 a medium quality and Tipo 5 the lower quality grade.
  • the slices are then glued to the corpus, and the stoppers brought into the right size and shape by cutting and sanding (to produce champagne stoppers) .
  • the tasting protocol is as follows: The bottles are divided, each type of wine separately, into groups of six bottles. The panel tastes the six bottles from group No.l, and decides whether the bottles have a uniform taste. If so, one bottle from group No .2 is tasted, and it is decided whether the taste of that bottle is identical to that of the six bottles from group No.l. If so, the remaining five bottles in group No.2 are tasted, and it is decided whether the taste of the five bottles is identical to the taste of the first bottle from group No.2. If so, the panel continues, tasting one bottle from group No.3, and so on.

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  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • Forests & Forestry (AREA)
  • Microbiology (AREA)
  • Mechanical Engineering (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Chemical And Physical Treatments For Wood And The Like (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

L'invention concerne un procédé de préparation d'articles en liège, plus particulièrement de bouchons de bouteilles de vin. Ce procédé consiste à traiter le liège avec une enzyme d'oxydation de phénol, de préférence, la laccase, peroxydase, catechol oxydase, o-aminophénol oxydase. Le traitement par l'enzyme d'oxydation de phénol réduit la tendance du liège à l'altération du goût/astringence affectant souvent le vin en bouteilles.
PCT/DK1999/000226 1998-05-13 1999-04-22 Traitement du liege avec une enzyme d'oxydation de phenol Ceased WO1999058309A1 (fr)

Priority Applications (6)

Application Number Priority Date Filing Date Title
ES99914448T ES2203104T3 (es) 1998-05-13 1999-04-22 Tratamiento del corcho con una enzima de oxidacion de fenoles.
AU33272/99A AU753129B2 (en) 1998-05-13 1999-04-22 Treatment of cork with a phenol oxidising enzyme
EP99914448A EP1077796B1 (fr) 1998-05-13 1999-04-22 Traitement du liege avec une enzyme d'oxydation de phenol
AT99914448T ATE244116T1 (de) 1998-05-13 1999-04-22 Behandlung von kork mit einem phenol-oxidierendem enzym
DE69909286T DE69909286D1 (de) 1998-05-13 1999-04-22 Behandlung von kork mit einem phenol-oxidierendem enzym
NZ508070A NZ508070A (en) 1998-05-13 1999-04-22 Treatment of cork with a phenol oxidising enzyme to reduce cork taint

Applications Claiming Priority (4)

Application Number Priority Date Filing Date Title
DK0656/98 1998-05-13
DK65698 1998-05-13
DKPA199900153 1999-02-05
DKPA199900153 1999-02-05

Publications (1)

Publication Number Publication Date
WO1999058309A1 true WO1999058309A1 (fr) 1999-11-18

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PCT/DK1999/000226 Ceased WO1999058309A1 (fr) 1998-05-13 1999-04-22 Traitement du liege avec une enzyme d'oxydation de phenol

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EP (1) EP1077796B1 (fr)
AR (1) AR013287A1 (fr)
AT (1) ATE244116T1 (fr)
AU (1) AU753129B2 (fr)
DE (1) DE69909286D1 (fr)
ES (1) ES2203104T3 (fr)
NZ (1) NZ508070A (fr)
PT (1) PT1077796E (fr)
WO (1) WO1999058309A1 (fr)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2001010614A1 (fr) * 1999-08-06 2001-02-15 Novozymes A/S Conglutination enzymatique de fragments de liege et procede de preparation d'articles de liege
DE102010002364A1 (de) 2009-02-25 2011-06-16 Hohenester, Hermann, Dr.Med.Vet. Mittel und deren Verwendung zur Behandlung von Naturstoffen

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1997011594A1 (fr) * 1995-09-25 1997-04-03 Biso B.V. Hache-paille pour broyer la paille derriere les dispositifs de separation des grains d'une moissonneuse batteuse
WO1997013628A1 (fr) * 1995-10-06 1997-04-17 Novo Nordisk A/S Blanchiment et sterilisation d'articles en liege

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1997011594A1 (fr) * 1995-09-25 1997-04-03 Biso B.V. Hache-paille pour broyer la paille derriere les dispositifs de separation des grains d'une moissonneuse batteuse
WO1997013628A1 (fr) * 1995-10-06 1997-04-17 Novo Nordisk A/S Blanchiment et sterilisation d'articles en liege

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2001010614A1 (fr) * 1999-08-06 2001-02-15 Novozymes A/S Conglutination enzymatique de fragments de liege et procede de preparation d'articles de liege
DE102010002364A1 (de) 2009-02-25 2011-06-16 Hohenester, Hermann, Dr.Med.Vet. Mittel und deren Verwendung zur Behandlung von Naturstoffen

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ATE244116T1 (de) 2003-07-15
AR013287A1 (es) 2000-12-13
AU753129B2 (en) 2002-10-10
DE69909286D1 (de) 2003-08-07
NZ508070A (en) 2002-06-28
AU3327299A (en) 1999-11-29
EP1077796B1 (fr) 2003-07-02
PT1077796E (pt) 2003-11-28
ES2203104T3 (es) 2004-04-01
EP1077796A1 (fr) 2001-02-28

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