EP1077796B1 - Behandlung von kork mit einem phenol-oxidierendem enzym - Google Patents

Behandlung von kork mit einem phenol-oxidierendem enzym Download PDF

Info

Publication number
EP1077796B1
EP1077796B1 EP99914448A EP99914448A EP1077796B1 EP 1077796 B1 EP1077796 B1 EP 1077796B1 EP 99914448 A EP99914448 A EP 99914448A EP 99914448 A EP99914448 A EP 99914448A EP 1077796 B1 EP1077796 B1 EP 1077796B1
Authority
EP
European Patent Office
Prior art keywords
cork
enzyme
stoppers
treatment
phenol oxidising
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.)
Expired - Lifetime
Application number
EP99914448A
Other languages
English (en)
French (fr)
Other versions
EP1077796A1 (de
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.)
Novozymes AS
Original Assignee
Novozymes 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 Novozymes AS filed Critical Novozymes AS
Publication of EP1077796A1 publication Critical patent/EP1077796A1/de
Application granted granted Critical
Publication of EP1077796B1 publication Critical patent/EP1077796B1/de
Anticipated expiration legal-status Critical
Expired - Lifetime legal-status Critical Current

Links

Classifications

    • BPERFORMING OPERATIONS; TRANSPORTING
    • B27WORKING OR PRESERVING WOOD OR SIMILAR MATERIAL; NAILING OR STAPLING MACHINES IN GENERAL
    • B27KPROCESSES, 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
    • B27K5/00Treating of wood not provided for in groups B27K1/00, B27K3/00
    • B27K5/04Combined bleaching or impregnating and drying of wood
    • BPERFORMING OPERATIONS; TRANSPORTING
    • B27WORKING OR PRESERVING WOOD OR SIMILAR MATERIAL; NAILING OR STAPLING MACHINES IN GENERAL
    • B27KPROCESSES, 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
    • B27K3/00Impregnating wood, e.g. impregnation pretreatment, for example puncturing; Wood impregnation aids not directly involved in the impregnation process
    • B27K3/002Impregnating wood, e.g. impregnation pretreatment, for example puncturing; Wood impregnation aids not directly involved in the impregnation process employing compositions comprising microorganisms
    • BPERFORMING OPERATIONS; TRANSPORTING
    • B27WORKING OR PRESERVING WOOD OR SIMILAR MATERIAL; NAILING OR STAPLING MACHINES IN GENERAL
    • B27KPROCESSES, 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
    • B27K7/00Chemical or physical treatment of cork
    • BPERFORMING OPERATIONS; TRANSPORTING
    • B67OPENING, CLOSING OR CLEANING BOTTLES, JARS OR SIMILAR CONTAINERS; LIQUID HANDLING
    • B67BAPPLYING CLOSURE MEMBERS TO BOTTLES JARS, OR SIMILAR CONTAINERS; OPENING CLOSED CONTAINERS
    • B67B1/00Closing bottles, jars or similar containers by applying stoppers
    • B67B1/03Pretreatment 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 Sea.
  • Wine corks are produced from reproduction cork, which is bark that has re-grown after the original bark has been stripped off the tree.
  • 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 sealing purposes at the inner bottom of various screw caps. Slices are usually cut perpendicular to the longitudinal direction of the cork slab.
  • At 50% of 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 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.
  • WO-A-97/11894 discloses a cork stopper for wine bottle which is coated with silicone rubber to prevent impurities in the cork from contaminating the contents of the bottle.
  • WO-A-97/13628 discloses that cork articles are bleached and/or sterilized firstly with an aqueous solution of hydrogen peroxide and subsequently with an aqueous solution of a catalase.
  • 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.
  • 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 in a second aspect, relates to the use of a cork or cork article for closing, sealing or stopping an object. And in a third aspect, the invention relates to a cork article (or cork) obtainable, in particular obtained, by any of the processes described herein.
  • 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 approach (van Oss C.J., M.K.Chaudhury and R.J.Good, 1987; Monopolar Surfaces; Advances in Colloid and Interface Science, 28, 35-64;).
  • 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.
  • 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 includes any oxidoreductase acting on phenols and 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.
  • 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,).
  • 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.
  • TCA 2,4,6-trichloro anisole
  • cork 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 worked up cork intermediate products (on the way to cork articles) are included in the definition of cork. Finally, the expression “cork” is also intended to cover the expression “cork articles.”
  • a "cork article” is an article which contains cork.
  • 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, 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 following the bleaching step, in particular following the drying step or the desinfection step, whatever the later.
  • the end user i.e. immediately before bottling a wine. It is preferably followed by a drying step (see above).
  • 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 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 Hyphomycetes, 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 alli or Dreschlera halodes.
  • DSM 2672 Fusarium oxysporum
  • Humicola insolens Trichoderma resii
  • Myrothecium verrucana IFO 6113
  • 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).
  • Basidiomycotina class Basidiomycetes
  • Coprinus cinereus f. microsporus IFO 8371
  • Coprinus macrorhizus e.g. NA-12
  • Trametes previously called Polyporus
  • T. versicolor e.g. PR4 28-A
  • 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-11.
  • 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 92/16634, or a variant thereof, e.g., a variant as described in WO 94/12621.
  • 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 Aspergillus, 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. C. plicatilis and C.
  • cinereus Psatyrella, Myceliophthora, e.g. M. 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.
  • 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 1 ⁇ 2 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 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 0.010-10mM, 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 WO 95/33836, Examples I-III;). The enzyme is added to water to obtain a concentration of 6.7 mg enzyme protein/l in the final treatment liquid.
  • 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.
  • a third reference is: Official Methods of Analysis of The Association of Official Agricultural Chemists, 10 th edition, 1965, p. 231-232.
  • a further, preferred, method is described in Am. J. Enol. Vitic. 1965, 16, 144-158; Singleton et al: "Colorimetry of total phenolics with phosphomolybdic-phosphotungstic acid reagents" , see in particular the preparation of the Folin-Ciocalteu reagent at p. 145, columns 1-2, as well as the paragraph headed "The improved method-precision and accuracy" at p. 156, 1 st column.
  • 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 setup 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.
  • 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 thus treated stoppers are used to seal bottles of two different kinds of German white wine. These bottles are then subjected to an accelerated ageing for 4 weeks: The bottles are kept in the refrigerator (5°C) during night, and at room temperature (20-25°C) during the day.
  • 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.1, 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.1. 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.

Landscapes

  • 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)

Claims (10)

  1. Verfahren zum Herstellen von Korkgegenständen, das den Schritt des Behandelns des Korks mit einem phenoloxidierenden Enzym umfasst.
  2. Verfahren, das die Behandlung des Korks mit einem phenoloxidierenden Enzym umfasst.
  3. Verfahren nach einem der Ansprüche 1-2, wobei das phenoloxidierende Enzym eine Phenoloxidase oder eine Peroxidase ist.
  4. Verfahren nach Anspruch 3, wobei die Phenoloxidase ausgewählt ist aus Katecholoxidase, Laccase oder o-Aminophenoloxidase.
  5. Verfahren nach Anspruch 1, wobei die Korkgegenstände ausgewählt sind aus Korkstopfen oder Korkscheiben.
  6. Verfahren nach einem der Ansprüche 1-2, das weiterhin ein oder mehrere der folgenden Schritte umfasst:
    i) ein Bleichen; und/oder
    ii) ein Trocknen; und/oder
    iii) eine Desinfektion.
  7. Kork oder Korkgegenstand erhältlich durch irgendein Verfahren nach Anspruch 1-6, wobei der Kork oder Korkgegenstand verminderte Korkflekken aufweist.
  8. Verwendung eines Korks oder Korkgegenstands nach Anspruch 7 zum Verschließen, Abdichten oder Verstopfen eines Objekts.
  9. Verwendung nach Anspruch 8, wobei das Objekt eine Flasche ist.
  10. Verwendung nach Anspruch 9, wobei das Objekt eine Wein- oder Sektflasche ist.
EP99914448A 1998-05-13 1999-04-22 Behandlung von kork mit einem phenol-oxidierendem enzym Expired - Lifetime EP1077796B1 (de)

Applications Claiming Priority (5)

Application Number Priority Date Filing Date Title
DK65698 1998-05-13
DK65698 1998-05-13
DK15399 1999-02-05
DKPA199900153 1999-02-05
PCT/DK1999/000226 WO1999058309A1 (en) 1998-05-13 1999-04-22 Treatment of cork with a phenol oxidising enzyme

Publications (2)

Publication Number Publication Date
EP1077796A1 EP1077796A1 (de) 2001-02-28
EP1077796B1 true EP1077796B1 (de) 2003-07-02

Family

ID=26063413

Family Applications (1)

Application Number Title Priority Date Filing Date
EP99914448A Expired - Lifetime EP1077796B1 (de) 1998-05-13 1999-04-22 Behandlung von kork mit einem phenol-oxidierendem enzym

Country Status (9)

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

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2001010614A1 (en) * 1999-08-06 2001-02-15 Novozymes A/S Enzymatic conglutination of cork fragments and enzymatic process for preparing cork articles
DE102010002364A1 (de) 2009-02-25 2011-06-16 Hohenester, Hermann, Dr.Med.Vet. Mittel und deren Verwendung zur Behandlung von Naturstoffen

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE19535175A1 (de) * 1995-09-25 1996-03-21 Jakobi Wilhelm Dipl Ing Fh Strohhäcksler zum Zerkleinern von Halmgut hinter den Kornabscheideeinrichtungen eines Mähdreschers
EP0853533A1 (de) * 1995-10-06 1998-07-22 Novo Nordisk A/S Bleichen und sterilizieren von korkartikeln

Also Published As

Publication number Publication date
NZ508070A (en) 2002-06-28
ATE244116T1 (de) 2003-07-15
WO1999058309A1 (en) 1999-11-18
AU3327299A (en) 1999-11-29
AU753129B2 (en) 2002-10-10
AR013287A1 (es) 2000-12-13
DE69909286D1 (de) 2003-08-07
EP1077796A1 (de) 2001-02-28
ES2203104T3 (es) 2004-04-01
PT1077796E (pt) 2003-11-28

Similar Documents

Publication Publication Date Title
US6152966A (en) Treatment of cork with a phenol oxidizing enzyme
Etiévant Wine
Pereira et al. Cork taint in wine: scientific knowledge and public perception—a critical review
Orth et al. Ubiquity of lignin-degrading peroxidases among various wood-degrading fungi
Rapp et al. Wine aroma
Tarko et al. The impact of oxygen at various stages of vinification on the chemical composition and the antioxidant and sensory properties of white and red wines
CA2316249C (en) Use of a phenol oxidising enzyme in the treatment of tobacco
Kheir et al. Impact of volatile phenols and their precursors on wine quality and control measures of Brettanomyces/Dekkera yeasts
Shraddha et al. Laccase: microbial sources, production, purification, and potential biotechnological applications
Moldes et al. Different proportions of laccase isoenzymes produced by submerged cultures of Trametes versicolor grown on lignocellulosic wastes
EP0953634B1 (de) Zusammensetzungen zur behandlung eines porösen gegenstandes, behandlungsverfahren und dessen verwendung
Lee et al. Microbiology and chemistry of cork taints in wine
Cheng et al. Purification of a new manganese peroxidase of the white-rot fungus Schizophyllum sp. F17, and decolorization of azo dyes by the enzyme
Sethuraman et al. Production of ligninolytic enzymes and synthetic lignin mineralization by the bird's nest fungus Cyathus stercoreus
HU216287B (hu) Fenolt oxidáló enzimrendszert, hidrogén-peroxid-forrást és a hatást fokozó szert alkalmazó fakító eljárás
Schmidt et al. Wood decay by the white-rotting basidiomycete Physisporinus vitreus from a cooling tower
Cosme et al. Wine stabilisation: An overview of defects and treatments
Nadaroglu et al. Purification and characterisation of laccase from Lactarius volemus and its application in removal of phenolic compounds from fruit juice
EP1077796B1 (de) Behandlung von kork mit einem phenol-oxidierendem enzym
US6045865A (en) Process for impregnating solid wood and product obtainable by the process
Giacosa et al. Relationships among electrolyzed water postharvest treatments on winegrapes and chloroanisoles occurrence in wine
ZA200006256B (en) Treatment of cork with a phenol oxidising enzyme.
Pickering et al. The production of reduced-alcohol wine using glucose oxidase-treated juice. Part II. Stability and SO2-binding
Morata et al. New trends in aging on lees
Petruzzi et al. Use of microfungi in the treatment of oak chips: possible effects on wine

Legal Events

Date Code Title Description
PUAI Public reference made under article 153(3) epc to a published international application that has entered the european phase

Free format text: ORIGINAL CODE: 0009012

17P Request for examination filed

Effective date: 20001031

AK Designated contracting states

Kind code of ref document: A1

Designated state(s): AT BE CH DE DK ES FI FR GB GR IE IT LI NL PT SE

17Q First examination report despatched

Effective date: 20020129

GRAH Despatch of communication of intention to grant a patent

Free format text: ORIGINAL CODE: EPIDOS IGRA

GRAH Despatch of communication of intention to grant a patent

Free format text: ORIGINAL CODE: EPIDOS IGRA

GRAA (expected) grant

Free format text: ORIGINAL CODE: 0009210

AK Designated contracting states

Designated state(s): AT BE CH DE DK ES FI FR GB GR IE IT LI NL PT SE

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: NL

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20030702

Ref country code: LI

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20030702

Ref country code: FI

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20030702

Ref country code: CH

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20030702

Ref country code: BE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20030702

Ref country code: AT

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20030702

REG Reference to a national code

Ref country code: GB

Ref legal event code: FG4D

REG Reference to a national code

Ref country code: CH

Ref legal event code: EP

REG Reference to a national code

Ref country code: IE

Ref legal event code: FG4D

REF Corresponds to:

Ref document number: 69909286

Country of ref document: DE

Date of ref document: 20030807

Kind code of ref document: P

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: SE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20031002

Ref country code: GR

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20031002

Ref country code: DK

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20031002

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: DE

Free format text: LAPSE BECAUSE OF FAILURE TO SUBMIT A TRANSLATION OF THE DESCRIPTION OR TO PAY THE FEE WITHIN THE PRESCRIBED TIME-LIMIT

Effective date: 20031003

NLV1 Nl: lapsed or annulled due to failure to fulfill the requirements of art. 29p and 29m of the patents act
REG Reference to a national code

Ref country code: CH

Ref legal event code: PL

REG Reference to a national code

Ref country code: ES

Ref legal event code: FG2A

Ref document number: 2203104

Country of ref document: ES

Kind code of ref document: T3

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: IE

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20040422

Ref country code: GB

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20040422

PLBE No opposition filed within time limit

Free format text: ORIGINAL CODE: 0009261

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: NO OPPOSITION FILED WITHIN TIME LIMIT

ET Fr: translation filed
26N No opposition filed

Effective date: 20040405

GBPC Gb: european patent ceased through non-payment of renewal fee

Effective date: 20040422

REG Reference to a national code

Ref country code: IE

Ref legal event code: MM4A

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: PT

Payment date: 20100405

Year of fee payment: 12

Ref country code: FR

Payment date: 20100421

Year of fee payment: 12

Ref country code: ES

Payment date: 20100429

Year of fee payment: 12

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: IT

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20100422

PGFP Annual fee paid to national office [announced via postgrant information from national office to epo]

Ref country code: IT

Payment date: 20100428

Year of fee payment: 12

PGRI Patent reinstated in contracting state [announced from national office to epo]

Ref country code: IT

Effective date: 20110616

REG Reference to a national code

Ref country code: PT

Ref legal event code: MM4A

Free format text: LAPSE DUE TO NON-PAYMENT OF FEES

Effective date: 20111024

REG Reference to a national code

Ref country code: FR

Ref legal event code: ST

Effective date: 20111230

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: PT

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20111024

Ref country code: FR

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20110502

PGRI Patent reinstated in contracting state [announced from national office to epo]

Ref country code: IT

Effective date: 20110616

REG Reference to a national code

Ref country code: ES

Ref legal event code: FD2A

Effective date: 20130605

PG25 Lapsed in a contracting state [announced via postgrant information from national office to epo]

Ref country code: ES

Free format text: LAPSE BECAUSE OF NON-PAYMENT OF DUE FEES

Effective date: 20110423