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Purification and Characterization of a Laccase from Cerrena unicolor and Its Reactivity in Lignin Degradation
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  • Purification and Characterization of a Laccase from Cerrena unicolor and Its Reactivity in Lignin Degradation
  • Purification and Characterization of a Laccase from Cerrena unicolor and Its Reactivity in Lignin Degradation
저자명
Kim. You-Sung,Cho. Nam-Seok,Eom. Tae-Jin,Shin. Woon-Sup
간행물명
Bulletin of the Korean Chemical Society
권/호정보
2002년|23권 7호|pp.985-989 (5 pages)
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대한화학회
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정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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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.