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 language | English |
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Pages (from-to) | 1040-1047 |
Number of pages | 8 |
Journal | Protein and Peptide Letters |
Volume | 17 |
Issue number | 8 |
DOIs | |
Publication status | Published - Aug 2010 |
User-Defined Keywords
- Mushroom
- Pleurotus cornucopiae
- laccase
- isolation