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

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

Volume: 17 Issue: 8

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

Affiliation:

Keywords: Mushroom, Pleurotus cornucopiae, laccase, isolation

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.

Cite this article as:

Ho Wong Jack, Bun Ng Tzi, Jiang Yun, Liu Fang, Cho Wing Sze Stephen and Yanbo Zhang Kalin, Purification and Characterization of a Laccase with Inhibitory Activity Toward HIV-1 Reverse Transcriptase and Tumor Cells from an Edible Mushroom (Pleurotus cornucopiae), Protein & Peptide Letters 2010; 17 (8) . https://dx.doi.org/10.2174/092986610791498966