• Korean Journal of Microbiology
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• v.36 no.3
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• pp.192-195
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• 2000

Degenerate primevs corresponding to the consensus sequences of the copper-binding regions in the N- and Cterminal domains of fungal laccases were used to isolate laccase gene-specific sequences froin a white rot rungus Ganodern~a lucidrm w-hich has been known to strengthen the imnnne system. A 1.6 Kbp fragment was amplified by PCR and its base sequence was detenuiued. Locating seven iutrous within the base sequence, we could deduce its amino acid sequence. The nucleotide sequence witl~out introlls was 47Y0 identical to that of lee1 gene of Pametes wllosa; lhe identity in amino acid sequences of the two was 7994 The deduced amino acid seqoence was also sunilar to those of Coriolus versicolo~ kc3 (79%); Co~,iolz~s hirsutus phenolouiduse (78%), Trainetes vel.srcoloi. lccl (77%), Trametes ~!i/Iosa Ice2 (77%) and Trametes vemicolor kc4 (66%).

• The Korean Journal of Mycology
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• v.20 no.1
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• pp.1-10
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• 1992

Fresh fungi were collected during field trips to Ullung Island from August, 1990, to September, 1991. Among them, some polyporoid fungi were recognized to the species. Thirty three species were identified, among which nine fungi were confirmed new in Korea and registered here with descriptions. These fungi are Auriporia aurulenta, Ceriporiopsis gilvescens, Ceriporiopsis subvermispora, Gloeophyllum trabeum, Junghuhnia separabilima, Oligoporus stipticus, Oxyporus similis, Phellinus lavigatus, and Polyporus melanopus.

• The Korean Journal of Mycology
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• v.32 no.2
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• pp.112-118
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• 2004

Laccase produced by Trametes hirsuta S1 isolated from Korea was partially purified and characterized using ultrafiltration, anion exchange chromatography and affinity chromatography. The laccase was produced as the predominant extracellular enzyme during primary metabolism. Neither lignin peroxidase nor veratryl alcohol oxidase (VAO) were detected in the culture fluid. Addition of 2,5-xylidine enhanced 4-fold laccase production. Purified laccase was a single polypeptide having a molecular mass of approximately 66 kDa, as determined by SDS-polyacrylamide gel electrophoresis, and carbohydrate content of 12%. $K_{m}\;and\;V_{max}$ values for laccase with ABTS [2,2-azinobis (3-ethylbenzthiazoline 6-sulfonic acid)] as a substrate (Lineweaver-Burk plot) was determined to $51.2\;{\mu}M\;and\;56.8\;{\mu}mole$, respectively. The optimal pH for laccase activity was found to be 3.0. The enzyme was very stable for 1 hour at $50^{\circ}C$. Half-life ($t_{1/2}$) of the enzyme was about 20 min at $70^{\circ}C$. Spectroscopic analysis of purified enzyme indicated that the enzyme was typical of copper-containing protein. Substrate specificity and inhibitor studies for laccase also indicated to be a typical fungal laccase. The N-terminal amino acid sequence of the T. hirsuta S1 laccase showed 100% of homology to those of laccase from C. hirsutus.