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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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 and Kalin Yanbo Zhang

Volume 17, Issue 8, 2010

Page: [1040 - 1047] Pages: 8

DOI: 10.2174/092986610791498966

Price: $65

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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