Purification and Characterization of a Laccase from Cerrena unicolor and Its Reactivity in Lignin Degradation

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 C...

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Bibliographic Details
Published in:Bulletin of the Korean Chemical Society 2002, Vol.23 (7), p.985-989
Main Authors: Kim, You-Sung, Cho, Nam-Seok, Eom, Tae-Jin, Shin, Woon-Sup
Format: Article
Language:Korean
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Summary: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.
ISSN:0253-2964
1229-5949