• Korean Journal of Microbiology
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• v.29 no.5
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• pp.267-269
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• 1991

The hyphal tip laccase of Coprinus congregatus which is a membrane-associated enzyme and shows diffdrdnt banding patterns of PAGE analysis when compared with the enzyme of liquid culture (Choi et al. 1987) has been successfully secreted to culture medium in liquid shake culture by lowering the pH of medium to 4.0. When the fungus is cultivated in YpSs(pH 4.0) liquid, only the hyphal tip laccase is found in the medium after 6 hr incubation and there is no liquid-type enzyme when examined by PAGE analysis.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.31 no.5
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• pp.1-11
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• 1999

Wood components, cellulose and lignin, are degraded simultaneously and the general outline for the complementary character of carbohydrates and lignin decomposition as well as the existence of enzymatic systems combining these processes is still valid. The degradatiion of free cellulose or hemicellulose into monosaccharides has long been known to be relatively simple, but the mechanism of lignin degradatiion wasn ot solved very clearly yet. Anyway the biodegradation of woold constituents is understood at present as an enzymatic process. Kigninolytic activity has been correlated with lignin and manganese peroxidases. At present the attention is paid to laccase. Laccase oxidizes lignin molecule to phenoxy radicals and quinones . This oxidation can lead to the cleavageo f C-C or C-O bonds in the lignin phenyl-propane subunits, resulting either in degradation of both side chains and aromatic rings, or in demethylation processes. The role of laccase lies in the "activation" of some low molecular weight mediators and radicals produced by fungal cultures. Such activated factors produced also in cooperation with other enzymes are probably exported to the wood environment where they work in degradation processes as the ' enzyme messengers." It is worth mentioning that only fungi possessing laccase show demethylating activity. Thus demethylation, the process important for ligninolysis, is probably caused exclusively by laccase. Under natural conditions laccase seems to work with other fungal enzymes , mediators and mediating radicals. It has shown the possibility of direct Bjrkman lignin depolymerization by cooperative activity of laccase and glucose oxidase.

• Journal of the Korean Wood Science and Technology
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• v.23 no.4
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• pp.27-32
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• 1995

To understand whether ligninolytic enzyme catalyze polymerization or depolymerization of the high molecular weight (HMW) lignin, the action of laccase and Mn-peroxidase (MnP) towards commercial ligninsulfonates (LS) was examined in various conditions of pH and cosubstrates. Polymerization occurred when LS was incubated with laccase at pH 6.0. In contrast, the high molecular weight portions were significant1y reduced at pH 4.5, especially when glucose was added. When LS was treated with MnP at pH 4.5, compounds of low molecular weight were produced. In particular, when cellobiose was added to Mn-P reaction mixture, the breakdown of LS was observed. In conclusion, degradation of LS by laccase and MnP occurred primarily at pH 4.5 where-as polymerization of LS was dominant at pH 6.0. Color index, however, was not greatly changed in the degradation mixtures of LS.

• Korean Journal of Microbiology
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• v.30 no.4
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• pp.252-259
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• 1992

Extracellular laccase excreted from Lentinus edodes ATCC 48085 was purified through a series of DEAF, Sephadex A-50. Con A-Sepharosc and Sephadex G-150 chromatography. Extracellular enzyme. which consists of a single polypeptide, has a n~olecular mass of 87.000 daltons and contains 12.0'%, carbohydrate. The N-terminal amino acid sequence (I5 residues) of the puritied enzyme was similar to that of laccases of PIeurotus ostreatus and Coriolus hirsutus. The enzyme showed optimal activity at near pH 4.8 and $40^{\circ}C$. The enzyme was stable at pH 7-9 and below $30^{\circ}C$. $K_{M}$ and $k_{cat}$ values for syringaldazine were estimated to be $0.4\mu\textrm{M}$ and 77 sec, respectively. The developed patterns of reaction products of thevenzyme on thin layer chromatography were similar to those of laccase of Pleurotus ostreatus.

• Korean Journal of Environmental Agriculture
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• v.25 no.3
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• pp.211-216
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• 2006

The present research was undertaken to investigate the activities of ligninolytic enzymes and dye-decolorization capabilities of white-rotting fungi Coriolus hirsutus LD-1. The isolated white-rotting fungi (Coriolus hirsutus LD-1) produced laccase (16,388.9 U/L) and manganese-dependent peroxidase (19.81 U/L) but it did not produce lignin peroxidase. When the isolated fungi was incubated with the treatment of dyes for 8 days, the rates of decolorization of remazol brilliant blue R and bromophenol blue were 70.2% and 98%, respectively. The activity for manganese-dependent peroxidase was low, whereas that for laccase was very high. Moreover, the laccase was more effective to decolor when compared to manganese-dependent peroxidase. The results suggested that laccase of Coriolus hirsutus LD-1 might be playing an important role in the decolorization of the dyes.

• Journal of Microbiology and Biotechnology
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• v.16 no.2
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• pp.226-231
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• 2006

Several white-rot fungi are able to produce extracellular lignin-degrading enzymes such as manganese peroxidase (MnP), lignin peroxidase (LiP), and laccase. In order to enhance the production of laccase and MnP using Trametes versicolor KCTC 16781 in suspension culture, the effects of major medium ingredients, such as carbon and nitrogen sources, on the production of the enzymes were investigated. The decolorization mechanism in terms of biodegradation and biosorption was also investigated. Among the carbon sources used, glucose showed the highest potential for the production of laccase and MnP. Ammonium tartrate was a good nitrogen source for the enzyme production. No significant difference in the laccase production was observed, when glucose concentration was varied between 5 g/l and 30 g/l. As the concentration of nitrogen source increased, a lower MnP activity was observed. The optimal C/N ratio was 25 for the production of laccase and MnP. When the concentrations of glucose and ammonium tartrate were simultaneously increased, the laccase and MnP activities increased dramatically. The maximum laccase and MnP activities were 33.7 U/ml at 72 h and 475 U/ml at 96 h, respectively, in the optimal condition. In this condition, over 90% decolorization efficiency was observed.

• Journal of the Korean Wood Science and Technology
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• v.26 no.3
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• pp.41-47
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• 1998

Some white-rot fungi, screened at the Laboratory of Forest Products Microbiological Chemistry, Chungbuk National University were cultured and added the inducer of laccase enzyme, 2,5-xylidine. The fungi named by CB-13, CB-20, CB-99, CB-100 and CB-123 strains showed positive results in the decolorization of aromatic compounds, carminic acid and Rhemazol brilliant blue R. Concerned to the inducing effect of 2,5-xylidine on laccase activity, CB-20, CB-100 and CB-123 strains showed very high activity by addition of 2,5-xylidine, whilst CB-13, CB-99 and CB-124 strains produced relatively high laccase enzymes, regardless of inducer addition. There were no any laccase activities on CB-25, CB-64 and CB-139, even in addition of inducer. It is confirmed that some screened fungi have decolorizing ability on aromatic compounds, carminic acid and Rhemazol brilliant blue R. Also, the addition of inducer, 2,5-xylidine, has increased the activity of laccase enzyme which is secreted from some white-rot fungi.

• Korean Journal of Microbiology
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• v.44 no.3
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• pp.199-202
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• 2008

A white rot fungus Irpex lacteus produced lignin degrading enzymes, which showed degrading activity against various recalcitrant compounds. However, laccase, one of the lignin degrading enzymes, was too low to be assayed by spectrophotometry using o-tolidine as the chromogenic substrate in this fungus under various culture conditions. A laccase expression vector was constructed using a cDNA from Phlebia tremellosa with the constitutively expressed promoter of glyceraldehydes-3-phosphate dehydrogenase gene, and introduced into I. lacteus by the restriction enzyme mediated integration transformation through the protoplast-$CaCl_2$ procedure. Two transformants showed highly increased laccase activities at the early growth phase in the minimal liquid medium, and they not only degraded bisphenol A, a notorious endocrine disrupting chemical, but also removed the estrogenic activity effectively.

• Journal of Microbiology and Biotechnology
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• v.28 no.8
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• pp.1360-1366
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• 2018

The fungi associated with termites secrete enzymes such as laccase (multi-copper oxidase) that can degrade extracellular wood matrix. Laccase uses molecular oxygen as an electron acceptor to catalyze the degradation of organic compounds. Owing to its ability to transfer electrons from the cathodic electrode to molecular oxygen, laccase has the potential to be a biocatalyst on the surface of the cathodic electrode of a microbial fuel cell (MFC). In this study, a two-chamber MFC using the laccase-producing fungus Galactomyces reessii was investigated. The fungus cultured on coconut coir was placed in the cathode chamber, while an anaerobic microbial community was maintained in the anode chamber fed by industrial rubber wastewater and supplemented by sulfate and a pH buffer. The laccase-based biocathode MFC (lbMFC) produced the maximum open circuit voltage of 250 mV, output voltage of 145 mV (with a $1,000{\Omega}$ resistor), power density of $59mW/m^2$, and current density of $278mA/m^2$, and a 70% increase in half-cell potential. This study demonstrated the capability of laccase-producing yeast Galactomyces reessii as a biocatalyst on the cathode of the two-chamber lbMFC.

• Journal of Microbiology
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• v.44 no.6
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• pp.617-621
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• 2006

Coprinellus congregatus secreted a laccase isozyme when the culture was transferred to an acidic liquid medium (pH 4.1). The laccase cDNA gene (clac2) was used as a probe for cloning of the genomic laccase gene (lac2) including the promoter (Plac2). The open reading frame (ORF) of lac2 had 526 deduced amino acids and four conserved copper binding domains as other fungal laccases. Recombinant plasmid (pRSlac2p-cDNA) of lac2 cDNA with its own promoter was transformed in Saccharomyces cerevisiae. Expression of the transformed lac2 gene was induced by oxidative stress ($H_2O_2$) in yeast and the survival rate of the transformed yeast strain was greatly increased when compared with that of the control strain transformed with pRS316 yeast vector.