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

Jack Ho Wong, Tzi Bun Ng*, Yun Jiang, Fang Liu, Stephen Cho Wing Sze, Kalin Yanbo Zhang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Pages (from-to)1040-1047
Number of pages8
JournalProtein and Peptide Letters
Volume17
Issue number8
DOIs
Publication statusPublished - Aug 2010
Externally publishedYes

User-Defined Keywords

  • Mushroom
  • Pleurotus cornucopiae
  • laccase
  • isolation

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