Purification and Characterization of a Laccase with Inhibitory Activity Toward HIV-1 Reverse Transcriptase and Tumor Cells from an Edible Mushroom (Pleurotus cornucopiae)

Author(s): Jack Ho Wong, Tzi Bun Ng, Yun Jiang, Fang Liu, Stephen Cho Wing Sze, Kalin Yanbo Zhang.

Journal Name: Protein & Peptide Letters

Volume 17 , Issue 8 , 2010

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Abstract:

A 66-kDa laccase, with an N-terminal sequence different from those of other mushroom laccases, was purified from fresh fruiting bodies of the edible mushroom Pleurotus cornucopiae by using affinity chromatography on Affi-gel blue gel, ion exchange chromatography on Mono Q and gel filtration on Superdex 75. The procedure resulted in a 16-fold purification and a specific enzyme activity of 17.3 U mg-1. The optimum pH and temperature for the purified laccase were pH 4 and 40°C, respectively. This laccase inhibited proliferation of murine leukemia cell line L1210 and human hepatoma cell line HepG2, and reduced the activity of HIV-1 reverse transcriptase with an IC50 of 22μM. There was neither mitogenic activity toward mouse splenocytes, nor hemagglutinating/hemolytic activity toward rabbit erythrocytes. This study yielded information about the potentially exploitable activities of P. cornucopiae laccase.

Keywords: Mushroom, Pleurotus cornucopiae, laccase, isolation

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Article Details

VOLUME: 17
ISSUE: 8
Year: 2010
Page: [1040 - 1047]
Pages: 8
DOI: 10.2174/092986610791498966
Price: $65

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