| Title |
Purification and Characterization of a Novel Laccase from the Edible Mushroom Hericium coralloides |
| Author |
Ya-Jie Zou1, He-Xiang Wang2, Tzi-Bun Ng3, Chen-Yang Huang1, and Jin-Xia Zhang1* |
| Address |
1Institute of Agricultural Resources and Regional Planning, Chinese Academy of Agricultural Sciences, Beijing 100081, P. R. China, 2State Key Laboratory for Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing 100193, P. R. China, 3Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, P. R. China |
| Bibliography |
Journal of Microbiology, 50(1),72-78, 2012,
|
| DOI |
|
| Key Words |
laccase, mushroom, Hericium coralloides, purification |
| Abstract |
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 IC50 of 0.06 μM. |
