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2000
Volume 17, Issue 8
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

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.

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/content/journals/ppl/10.2174/092986610791498966
2010-08-01
2025-08-16
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  • Article Type:
    Research Article
Keyword(s): isolation; laccase; Mushroom; Pleurotus cornucopiae
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