Purification and characterization of a novel laccase from the edible mushroom Hericium coralloides

文献类型: 外文期刊

第一作者: Zou, Ya-Jie

作者: Zou, Ya-Jie;Huang, Chen-Yang;Zhang, Jin-Xia;Wang, He-Xiang;Ng, Tzi-Bun

作者机构:

关键词: Hericium coralloides;laccase;mushroom;purification

期刊名称:JOURNAL OF MICROBIOLOGY ( 影响因子:3.422; 五年影响因子:3.28 )

ISSN:

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收录情况: SCI

摘要: A novel laccase from the edible mushroom Hericium coralloides was purified by ion exchange chromatography on diethylaminoethyl (DEAE) cellulose, carboxymethyl (CM) cellulose, and Q-Sepharose columns followed by fast protein liquid chromatography gel filtration on a Superdex 75 column. Analysis by gel filtration and SDS-PAGE indicated that the protein is a monomer in solution with a molecular mass of 65 kDa. Its N-terminal amino acid sequence was AVGDDTPQLY, which exhibits partial sequence homology to previously isolated laccases. Optimum activity was observed at pH 2.2 and at 40°C. The enzyme showed activity toward a variety of substrates, the most sensitive of which was 2,2′-azinobis [3-ethylbenzothiazolone-6-sulfonic acid] diammonium salt (ABTS). The degradation activity toward substrates was ABTS > N,N-dimethyl-1,4-phenylenediamine > catechol > 2-methylcatechol > pyrogallol. The laccase did not exert any antiproliferative activity against Hep G2 or MCF 7 tumor cell lines at a concentration of 60 μM, unlike some previously reported mushroom proteins, but showed significant activity toward human immunodeficiency virus-1 (HIV-1) reverse transcriptase with an IC _(50) of 0.06 μM.

分类号: Q93

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