Production of laccase from Trametes trogii TEM H2: a newly isolated white-rot fungus by air sampling.
ABSTRACT This work represents the first report of isolation of potential laccase producers by air sampling using media supplemented with 2,2-azinobis (3-ethylbenzothiazoline-6-sulfonate) and guaiacol for laccase production and secretion indicators. Nine fungal isolates showed positive reactions with 2,2-azinobis (3-ethylbenzothiazoline-6-sulfonate) and guaiacol. The isolate named TEM H2 exhibited the largest and intensive oxidation zones with 2,2-azinobis (3-ethylbenzothiazoline-6-sulfonate) (85 mm) and guaiacol (66 mm) and therefore it was selected for detailed investigations. The strain was identified as Trametes trogii TEM H2 due to the morphological characteristics and the comparison of internal transcribed spacer ribosomal DNA gene sequences. The laccase production was screened in different liquid cultures. The best laccase production medium was determined as soluble starch yeast extract medium in which laccase production was reached to a maximum level (989.6 U l(-1) ) on the 8(th) day of cultivation. Effects of different initial pH values on laccase production were tested. Optimum pH value for laccase production in soluble starch yeast extract medium was determined as pH 3.0 with 15425.0 U l(-1) laccase production at 12(th) day of cultivation. In addition, effects of eight inducers (veratryl alcohol, ferulic acid, 1-Hydroxybenzotriazole, syringic acid, 2,2-azinobis (3-ethylbenzothiazoline-6-sulfonate), 1 mmol l(-1) CuSO(4) , 3% ethanol, guaiacol) were examined. Only cultures with 2,5-xylidine exhibited 1.9 fold increase in laccase activity reaching to 28890.0 U l(-1) . (© 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim).
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ABSTRACT: A new lignin-degrading basidiomycete, strain PM1 (= CECT 2971), was isolated from the wastewater of a paper factory. The major ligninolytic activity detected in the basidiomycete PM1 culture supernatant was a phenoloxidase (laccase). This activity was produced constitutively in defined or complex media and appeared as two protein bands in native gel electrophoresis preparations. No enzyme induction was found after treatment with certain potential laccase inducers. Laccase I was purified to homogeneity by gel filtration chromatography, anion-exchange chromatography, and hydrophobicity chromatography. The enzyme is a monomeric glycoprotein containing 6.5% carbohydrate and having a molecular weight of 64,000. It has an isoelectric point of 3.6, it is stable in a pH range from 3 to 9, and its optimum pH is 4.5. The laccase optimal reaction temperature is 80 degrees C, the laccase is stable for 1 h at 60 degrees C, and its activity increases with temperature. Spectroscopic analysis revealed that the enzyme has four bound copper atoms, a type I copper, a type II copper, and a type III binuclear copper. The amino-terminal sequence of the protein is very similar to the amino-terminal sequences of laccases from Coriolus hirsutus and Phlebia radiata.Applied and Environmental Microbiology 09/1993; 59(8):2607-13. · 3.68 Impact Factor
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ABSTRACT: The white-rot fungus Trametes trogii excretes a main laccase showing a molecular mass of 70 kDa, acidic isoelectric point and N-terminal sequence homologous to that of several phenol oxidases. The purified enzyme oxidizes a number of phenolic and non-phenolic compounds; recalcitrant molecules may be converted into substrates by introducing, in the correct position, o- or p-orienting ring-activating groups.Applied Microbiology and Biotechnology 06/1998; 49(5):545-51. · 3.69 Impact Factor
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ABSTRACT: The sources of ligninocellulose that occur in various forms in nature are so vast that they can only be compared to those of water. The results of several, more recent experiments showed that laccase probably possesses the big ability for "lignin-barrier" breakdown of ligninocellulose. The degradation of this compound is currently understood as an enzymatic process mediated by small molecules, therefore, this review will focus on the role of these mediators and radicals working in concert with enzymes. The fungi having a versatile machinery of enzymes are able to attack directly the "lignin-barrier" or can use a multienzyme system including "feed-back" type enzymes allowing for simultaneous transformation of lignin and carbohydrate compounds.Journal of Basic Microbiology 02/2001; 41(3-4):185-227. · 1.20 Impact Factor