WO2012023021A1 - Method for obtaining laccase enzyme from arthrographis sp. - Google Patents
Method for obtaining laccase enzyme from arthrographis sp. Download PDFInfo
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- WO2012023021A1 WO2012023021A1 PCT/IB2011/001856 IB2011001856W WO2012023021A1 WO 2012023021 A1 WO2012023021 A1 WO 2012023021A1 IB 2011001856 W IB2011001856 W IB 2011001856W WO 2012023021 A1 WO2012023021 A1 WO 2012023021A1
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- laccase
- enzyme
- arthrographis
- dyes
- nearly
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Classifications
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38654—Preparations containing enzymes, e.g. protease or amylase containing oxidase or reductase
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0055—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10)
- C12N9/0057—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10) with oxygen as acceptor (1.10.3)
- C12N9/0061—Laccase (1.10.3.2)
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- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
- D06L4/40—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using enzymes
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
- D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
- D06P5/15—Locally discharging the dyes
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06P—DYEING OR PRINTING TEXTILES; DYEING LEATHER, FURS OR SOLID MACROMOLECULAR SUBSTANCES IN ANY FORM
- D06P5/00—Other features in dyeing or printing textiles, or dyeing leather, furs, or solid macromolecular substances in any form
- D06P5/15—Locally discharging the dyes
- D06P5/158—Locally discharging the dyes with other compounds
Definitions
- This invention relates to a method for obtaining laccase enzyme from Arthrographis sp.MTCC5479 and applications thereof.
- Laccase (benzenediol: oxygen oxidoreductase EC 1.10.3.2) is a polyphenol oxidase and belongs to a group of enzymes known as multi-copper oxidases. Laccases have one type-1 copper atom, which shows absorbance at 600 nm and imparts blue color to the enzyme. Apart from one type-1 copper atom, laccase have one type-2 and two type-3 copper atoms per enzyme molecule. Laccase catalyze the four electron reductions of molecular oxygen to water accompanied by the oxidation of a substrate [ 1 ] .
- Laccase enzyme was first reported to occur in the Japanese lacquer tree, Rhus vernicifera in 1883. The enzyme was later found to occur in fungi known as 'white rot fungi' belonging to the class Basidiomycetes. It includes genera Agaricus, Cyathus, Lentinus, Phlebia, Partus, Pleurotus and Trametes. A few fungi belonging to the class Ascomycetes such as Curvularia, Gaeumannomyces, Mauginella, and Melanocarpus also produce laccase [2].
- Laccase is an economically important enzyme because of its ability to oxidize range of xenobiotic compounds. Laccase exhibit broad substrate specificity and can catalyze oxidation of polyphenols, methoxy-substituted phenols, aminophenol and their derivatives [3]. Laccase catalyze various oxidation reactions, which are useful in paper and pulp industry [4], in food and beverage industry [5], bioremediation [6], biosensors [7,8] and bio-fuel cells [9]. Economical availability of purified laccase is an important factor for usage of laccase in industry [5]. White rot fungi belonging to the class Basidiomycetes are the major source of laccase enzyme. However, extracellular level of laccase enzyme produced by these fungi is low [10].
- laccase of Basidiomycetes Cloning and expression of laccase of Basidiomycetes in a recombinant host is beset by problems, such as different codon usage, missing chaperone and post translational modifications [1 1]. Specific activity of laccase enzyme is dependent on the redox potential of laccase enzyme. Laccase produced in a recombinant host tends to have a lower redox potential than their counterparts produced by the wild strain [12]. Hence, it is important to explore microbial diversity for novel laccase producing strains having higher laccase yield and laccase enzyme with higher specific activity and higher redox potential.
- laccase genes from such fungus can also preferably be cloned and expressed efficiently in fungal hosts, such as Pichia or Aspergillus for their large scale production.
- Patent No.7,927,849B2 has disclosed a method for production of laccase enzyme from Thielavia species [13].
- the highest activity obtained reported in the patent document is 20 nkatal ml "1 within six days.
- the specific activity of the enzyme using ABTS as substrate is 1020 nkatl/mg.
- laccase enzyme with high specific activity and yield.
- the laccase enzyme is produced by a fungal strain belonging to the class Ascomycetes.
- the laccase produced by the novel fungus according to the method disclosed herein can be applied for various laccase catalyzed biochemical reactions in diverse areas of applications, such as degradation of textile dyes in the effluent, treatment of the denim for bleaching and removal of back staining and bioremediation in general, such as degradation of some pollutants like polyaromatic hydrocarbons (PAH) and xenobiotics.
- PAH polyaromatic hydrocarbons
- the applications of laccase also exist in bakery, brewery and wine industry, in synthesis of chemicals, fabrication of cathode for fuel cell.
- the objective of the present invention is to provide a method for obtaining laccase enzyme from Arthrographis sp.MTCC5479. SUMMARY OF THE INVENTION
- the present invention provides a method for obtaining laccase enzyme from Arthrographis sp. MTCC5479 ( Figure 1 and 2).
- the novel laccase enzyme is secreted into the medium by the producer strain belonging to the genus, Arthrographis.
- the yield of the enzyme under the conditions described herein is 9-14 IU ml "1 or 150- 250 nktal ml "1 when assayed using 1 mM ABTS in 50 mM Mcllvain buffer, pH 4.0 at 30°C. ( Figure 3).
- the extracellular laccase produced by Arthrographis sp. can be isolated and purified easily from the culture filtrate.
- the enzyme is active in the wide pH range from 3-8.
- the pH optimum lies in the range of 3 to 6 for various common substrates, such as 2,2'azinobis-3-ethylbenzthiazole-6-sulphonate (ABTS), guaiacol, 2-methoxyphenol(guaiacol), 2,6 dimethoxyphenol (DMP), syringaldazine and indigo.
- ABTS 2,2'azinobis-3-ethylbenzthiazole-6-sulphonate
- guaiacol 2-methoxyphenol(guaiacol)
- DMP 2,6 dimethoxyphenol
- syringaldazine indigo.
- the enzyme is active in the range of 25°C to 70°C; however, the optimum temperature of the enzyme is in the range of 40°C to 50°C for various substrates.
- the molecular weight of the enzyme is about 63 kDa, as determined by SDS-PAGE ( Figure 4 & 5).
- the molecular weight of the enzyme by MALDI-ToF is 58.33 kDa ( Figure 6).
- the isoelectric point of the enzyme (pi) is about 3.5 as determined by isoelectric focusing ( Figure 7).
- the N-terminal amino acid sequence of the enzyme is Gly-Ile- Gly-Pro-Val-Thr-Asp-Leu-Thr-Ile-Ser-Asn-Ala-Glu-Val .
- the specific activity of Arthrographis laccase is 347 IU mg "1 (5784 nkatal mg "1 ) against ImM ABTS in 50 mM Mcllvain buffer, pH 4.0 at 30 °C.
- Arthrographis laccase measured by kinetic method using 0.02 mM syrigaldazine as the substrate in 50 mM Mcllvain buffer, pH 5.5 at 30 °C is 6380 IU mg "1 (10635 nkatal mg ⁇ .
- the enzyme can efficiently degrade various textile dyes belonging to anthroquinone group, azo group, triarylmethane group, eurhodin group, and reactive dyes. Presence of specific mediators, such as 1 -hydroxybenzotriole, violuric acid, methylsyringate and acetosyringone, the rate of degradation of dyes is significantly enhanced.
- indigo vat blue
- ABTS 2,2'azinobis-3-ethylbenzthiazole-6- sulphonate
- the enzyme may also be employed in applications which exists in food industry, in brewery and wine industry, in paper and pulp industry, in synthesis of chemicals, and fabrication of cathode for fuel cell and where, the laccase enzyme is known to have been used.
- Arthrographis laccase is capable of oxidizing indigo dye (Vat Blue) in the presence of mediators such as acetosyringone (4'-Hydroxy-3', 5'-dimethoxyacetophenone) and 2, 2'azinobis-3-ethylbenzthiazole-6-sulphonate (ABTS).
- mediators such as acetosyringone (4'-Hydroxy-3', 5'-dimethoxyacetophenone) and 2, 2'azinobis-3-ethylbenzthiazole-6-sulphonate (ABTS).
- ABTS 2, 2'azinobis-3-ethylbenzthiazole-6-sulphonate
- step a innoculating production medium containing flasks with strain obtained in step a
- step b incubating the medium obtained in step b, at 30°C on rotary shaker at the speed of about 180 rpm for nearly 72 hrs.
- step c inducing the culture obtained in step c after 72 hrs with Xylidine 0.00001 to 0.0001% (v/v), CuS0 4 .5H 2 0, 0.0025 to 0.025% (w/v) or 100 ⁇ to 1000 ⁇ ,
- step d incubating the culture obtained in step d at nearly 30°C for about 12-15 days.
- step f withdrawing of culture obtained in step e, and separating Laccase enzyme excreted into the medium from cell mass by centrifugation at nearly 8000 X g for nearly 10 minutes.
- step f concentrating and purifying the enzyme obtained in step f by methods described herein.
- the yield of laccase enzyme ranges from 9-14 IU/ml.
- laccase enzyme is characterized in having : I. Molecular weight nearly 63kDa, by SDS-PAGE, or 58.33 by MALDI-
- N-terminal amino acid sequence having Seq ID. No.l In another embodiment of the present invention wherein the enzyme functions at pH 2.5 to 8.5, preferably at pH 3 to 5.5.
- the enzyme preparation is in the form of liquid, powder or granulate after blending or mixing with inert substances or salts in order to increase its shelf life.
- the enzyme is useful for degradation of textile dyes including azo, anthraquinone, triphenylmethane, indigoid, triazine and eurhodin groups of dyes in individual or in a mixture form of these dyes.
- the laccase enzyme is isolated from Arthrographis sp., and is useful for removing stains, for bleaching of pulp, for treating of fibers for whitening, for coloring of animal hairs including wool for treating of textile dye or dyes in effluents, for fabrication of cathode in a fuel cell, for formulations of coatings and adhesives based on polymerization of phenolic monomers etc.
- FIGURE 1 Colony of Arthrographis sp.MTCC5479 on YPD agar
- Molecular weight markers used were Phosphorylase b (97kDa), Bovine Serum Albumin(67kDa), Ovalbumin (45kDa) and Carbonic anhydrase. (30kDa).
- Laccase enzyme was produced by growing Arthrographis strain in sterile liquid culture medium comprising
- the fungal strain Arthrographis sp.MTCC5479 was grown on yeast, peptone and dextrose (YPD) agar plates and incubated for 6-7 days. Mycelial mass and spores were collected from the plate by scrapping surface of agar plate wth a sterile loop and inoculated into the 500 ml flask containing 100 ml YPD medium and was incubated at 30 °C for 3 days. The cell mass obtained was used as inoculum to inoculate 10 flasks containing 500 ml of production medium. Innoculated production medium containing flasks were incubated at 30°C on rotary shaker at the speed of 180 rpm for 72 hrs.
- YPD yeast, peptone and dextrose
- Laccase enzyme excreted into the medium was separated from cell mass after peak of enzyme activity was reached after about 12-15 days of incubation at 30°C. Extra cellular enzyme activity obtained is in the range of 9-14 IU ml "1 of the culture broth ( Figure 3).
- laccase from Arthrographis laccase was demonstrated in shake flasks, other suitable containers for the production of the laccase such as trays or fermenters may be used for this purpose by those skilled in the art of microbial fermentation.
- the ultrafiltrate (180 ml) was loaded on to Q-Sepharose column (40 ml) equilibrated at pH 5.5 using 50 mM sodium acetate buffer and eluted using 0-50% linear gradient of 500 mM sodium chloride in the same buffer. Active fractions were pooled and precipitated by 100% saturation of ammonium sulphate. The precipitate was loaded on Sephacryl S-200
- Laccase activity was measured by end point spectrophotometric method. Conditions for assay were as given below. The assay was conducted in the temperature controlled cuvette chamber of spectrophotometer (Analytica Jena SPECORD 600).
- One unit of enzyme activity was defined as the amount of enzyme oxidizing 1 ⁇ ABTS per minute under these conditions.
- Laccase activity was measured by kinetic spectrophotometric method. Conditions for assay were as given below. The assay was conducted in the temperature controlled cuvette chamber of spectrophotometer (Analytica Jena SPECORD 600).
- Protein content of enzyme preparations were estimated according to the method of Bradford using Bradford reagent (B-6916, Sigma chemicals, USA) and solution of known concentration of bovine serum albumin as the protein standard.
- Specific activity of purified enzyme preparation was determined in terms of International Units per milligram of protein IU mg "1 . Enzyme activity was measured as given in example 3 and 4. Protein content was estimated as given in example 5. Specific activity in terms of derived SI units nkatal can be calculated by multiplying the international units by the factor 16.67.
- Mcllvaine buffer (Citrate-Phosphate) buffer at the concentration of 50 mg/L.
- These dyes include dyes belonging to azo group, anthroquinone group, acridine group, eurhodin group, and reactive dye. 20 ml solution of dye was taken in a flask of 100 ml volume.
- Crude enzyme in form of ultrafiltrate was added to the dye solution to make final enzyme activity about 100 Units/mL.
- One more set of dye solution was also set.
- Hydroxybenzotriazole (HOBT) a mediator molecule was added to the concentration of 5.0 mM.
- Flasks were incubated at 30 °C. Residual dye contents were estimated after 12 hrs and 24 hrs. of incubation.
- Flasks containing the mediator 1-HOBT showed more than 90% decolorization of Acridine orange, Brilliant blue, Cibacron Blue, Rose Bengal, Erythrosine, Malachite green, Neutral red, Bromophenol blue Remazol brilliant blue, Crystal violet, Congo red Rhodamine B and Cotton Blue within 12 hrs.
- laccase from Arthrographis sp. for degradation of textile dyes is not limited only the number of dyes listed above.
- the above experiment only demonstrates the versatility of Arthrographis laccase to degrade textile dyes belonging to different groups.
- the enzyme from Arthrographis sp can be applied to the degradation of dyes other than being mentioned herein by a person skilled in the art of use of laccase enzyme and different mediators for the reaction carried out by the enzyme.
- the enzyme may also be applied for the purpose of degradation of dyes in a suitable reactor where contact of dyes and enzymes can take place.
- a piece of desized denim cloth was obtained from Rossari Biotech India Pvt. Ltd, Mumbai, India. The cloth was rinsed with tap water and cut into approximately 1 square inch swatches (dry weight about 800-900 mg) Denim swatch in were submerged in 25 ml Mcllvaine buffer, pH 3.0 contained in 100 ml conical flask. Redox mediator acetosyringone (4'-Hydroxy-3', 5'-dimethoxyacetophenone) and 2, 2'azinobis-3-ethylbenzthiazole-6-sulphonate (ABTS) were added in two flasks separately at the concentration of 1-5 mg ml "1 .
- Redox mediator acetosyringone (4'-Hydroxy-3', 5'-dimethoxyacetophenone
- ABTS 2, 2'azinobis-3-ethylbenzthiazole-6-sulphonate
- Stone washed denim fabric was obtained from local market. Denim was cut into about 1 square inch. The stone washed (dry weight about 800-900.mg) Denim swatches in were submerged in 25 ml Mcllvaine buffer, pH 3.0 contained in 100 ml conical flask. Redox mediator acetosyringone (4'-Hydroxy-3', 5'-dimethoxyacetophenone) and 2,2'azinobis-3-ethylbenzthiazole-6-sulphonate (ABTS) were added in two flask separately at the concentration of 1 -5 mg ml "1 .
- Redox mediator acetosyringone (4'-Hydroxy-3', 5'-dimethoxyacetophenone
- ABTS 2,2'azinobis-3-ethylbenzthiazole-6-sulphonate
- ABTS was added as dry powder whereas, acetosyringone was added as solution in ethanol (50 mg/ml).
- the denim swatches in flasks were allowed to imbibe the buffer and mediator for 5 minutes.
- Arthrographis laccase 25 IU was added to each flask in order to initiate the reaction.
- the flasks were incubated in a rotary shaker at 45°C, 180-rpm speed. After 90 min the denim swatches were removed form the flasks, rinsed with water blot dried using filter paper ironed. The results were photographed ( Figure 10).
- Examples given in 8 and 9 demonstrate efficacy of Arthrographis laccase in bleaching denim for obtaining faded look effect or enhancing contrast in the stonewashed denim
- laccase from Arthrographis laccase can also be applied for treatment of garments made from denim fabric by a person skilled in the art of use of laccase enzymes for bleaching.
- Enzyme partially purified by ion exchange chromatography method as described in example 2 were dialyzed against 50 mM citrate phosphate buffer pH 6.0.
- the enzyme solution was concentrated to reduce its volume using Amicon centrifugal ultrafiltration devices.
- the concentrated enzyme solution had activity of 1200 IU per ml.
- Q- Sepharose was packed in a column and equilibrated at pH 6.0 and then transferred into a 25 ml flask. 20 ml of concentrated solution of laccase containing 1220U ml "1 was added to 2 ml Q-Sepharose equilibrated at pH 6.0 and allowed to bind it for 30 min.
- the unbound enzyme was removed from the Q-Sepharose by filtering was the passed through Whatman number 1 filter paper.
- the Sepharose with enzyme adsorbed on it was suspended in the buffer pH 6.0 containing ImM 1,3-Propylenediamine and was incubated for 1 hour at room temperature. After 1 hr 1, 4-Butanediol Diglycidyl Ether (BDDGE) was added in the suspension and was mixed by inverting tube several times. The quantity of 1, 4-Butanediol diglycidyl ether (BDDGE) may range from 0.05 mM to 10 mM. The suspension was then kept at room overnight and then washed with citrate phosphate buffer pH 4.0 The sepharose was then suspended in phosphate buffer pH 6.0 containing 1 mM Glycyl-glycine and incubated for 6 hrs at room temperature. After this treatment for blocking free oxirane groups, the suspension was again washed with 50 mM Citrate phosphate buffer pH 4.0. Final activity of the immobilized laccase preparation was 10,000 IUgm "1 .
- the wine was then first filtered through Whatman Number 1 filters paper and then through 0.5-micron filter.
- Initial and residual phenolics content were determined by Denis method, using tannic acid as model phenolic compound. Reduction in phenolics contents by laccase treatment was 3 fold.
- Laccase produced using Arthrographis strain is not repressible by glucose or nitrogen sufficiency.
- Laccase production is under submerged fermentation as well as solid-state culture.
- Laccase produced is extracellular, with a high yield of 10,000 to 20,000 IU per liter of the culture supernatant and can be easily purified from the culture supernatant.
- Laccase produced offers broad specificity in dye degradation.
- the cell free enzyme is capable of degradation of dyes belonging to diverse groups of dyes such as azo dyes, triphenylmethane dyes, reactive dyes, anthroquinone dyes, eurhodin dyes and acridine dyes.
- the Arthrographis laccase treatment of Denim is capable of creating a heavy faded look on denim when, ABTS is used as a mediator for denim bleaching. This provides an alternative to the use of hypochlorite treatment for creating heavy faded look on denim.
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DE112011102717T DE112011102717T5 (en) | 2010-08-17 | 2011-08-12 | Method of obtaining the laccase enzyme of Arthrographis sp. |
CN201180039782.4A CN103270154B (en) | 2010-08-17 | 2011-08-12 | A kind of method obtaining laccase from Arthrographis bacterial classification |
BR112013003725-3A BR112013003725B1 (en) | 2010-08-17 | 2011-08-12 | METHOD FOR OBTAINING LACASE ENZYME FROM ARTHROGRAPHIS SP |
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IN1951/DEL/2010 | 2010-08-17 | ||
IN1951DE2010 | 2010-08-17 |
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BR (1) | BR112013003725B1 (en) |
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WO2001083761A1 (en) * | 2000-04-28 | 2001-11-08 | Novozymes A/S | Laccase mutants |
US7927849B2 (en) | 2004-09-21 | 2011-04-19 | Ab Enzymes Oy | Laccase enzyme and use thereof |
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WO1998038287A1 (en) * | 1997-02-28 | 1998-09-03 | Novo Nordisk A/S | Laccase mutants |
CN101407794B (en) * | 2008-11-28 | 2013-09-11 | 昆明理工大学 | Laccase inducer and use thereof for improving microbial laccase production ability |
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- 2011-08-12 CN CN201180039782.4A patent/CN103270154B/en not_active Expired - Fee Related
- 2011-08-12 WO PCT/IB2011/001856 patent/WO2012023021A1/en active Application Filing
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WO2001083761A1 (en) * | 2000-04-28 | 2001-11-08 | Novozymes A/S | Laccase mutants |
US7927849B2 (en) | 2004-09-21 | 2011-04-19 | Ab Enzymes Oy | Laccase enzyme and use thereof |
Non-Patent Citations (16)
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SIGOILLOT, C., RECORD, E., BELLE, V., ROBERT, J.L., LEVASSEUR, A., PUNT, P. J., VAN DEN HONDEL, C.A., FOURNEL, A., SIGOILLOT, J. C: "Natural and recombinant fungal laccases for paper pulp bleaching", APPL. MICROBIOL. BIOTECHNOL., vol. 64, 2004, pages 346 - 352 |
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