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.
Citations
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