• Microbiology and Biotechnology Letters
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• v.14 no.2
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• pp.139-143
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• 1986

The production media and enzymatic characteristics of laccase from Ganoderma lucidum was investigated. Potato dextrose yeast extract media was proved to be the best for laccase production. The enzyme has optimum pH of 6.45km value of 6.71 mM and appeared to be stable at wide pH range. The enzyme was inactivated partially by methanol and ethanol and totally by sodium azide but not at all by acetone. Also the enzyme purification was performed and the data is given.

• Applied Biological Chemistry
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• v.38 no.6
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• pp.490-495
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• 1995

Among the cellulases by Cellulomonas sp. KL-6. CMCase and filter paperase, which were produced as the out enzymes of cell, had been much produced, but very small amounts of ${\beta}-glucosidase $, the enzyme of which is cell bound form, was produced by this organism. The optimal culture times for CMCase and filter paperase productions were 5 days, while that of ${\beta}-glucosidase$ was 4 days. When this strain was cultured under the optimal medium for enzyme production, CMCase, FPase and ${\beta}-glucosidase$ were $82\;units/m{\ell},\;80\;units/m{\ell}\;and\;1.2\;units/m{\ell}$, respectively. Thus these results were showed to increase enzyme productivities as about $60{\sim}70%$ than those produced in basal medium. $CaCO_3$ injected to the medium as the ratio of 0.1% was not only enhanced cellulase activities but also effective as acid neutralizing agent. The production effects of lignase and lactase by this bacterium in filter paper medium was not appeared.

• Bulletin of the Korean Chemical Society
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• v.23 no.7
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• pp.985-989
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• 2002

For efficient biopulping process, very active and stable lignase is essential. Laccase is one of the best enzyme in terms of environmentally benign processes, since the enzyme uses oxygen as an oxidant to degrade lignin and produces no hamful prod ucts. We could purify a laccase homogeneously from Cerrena unicolor in a very active state. It shows characteristic absorption feature with blue band at λmax = 604 ㎚. Molecular weight of the enzyme is 57,608 which could be accurately determined by MALDI/TOF MS. The enzyme has 2.8 copper ions per enzyme implying apoenzymes might exist together. The enzyme is active in lignin degradation and the activity increases 4 times in the presence of ABTS as a mediator.