Abstract
A novel peroxidase has been isolated from fresh fruiting bodies of the mushroom Pleurotus pulmonarius, with a purification protocol of ion exchange chromatography on DEAE-cellulose, affinity chromatography on ConA-Sepharose, ion exchange chromatography on CM-cellulose, and gel filtration by FPLC on Superdex 75. The peroxidase was unadsorbed on either DEAE-cellulose or ConA-Sepharose, but was adsorbed on CM-cellulose. It exhibited a molecular mass of 55 kDa in gel filtration and also in sodium dodecyl sulfate–polyacrylamide gel electrophoresis, indicating that it is a monomeric protein. It possessed a distinctive N-terminal amino acid sequences from other isolated mushroom peroxidases. The optimal pH and temperature for the enzyme were 4.0 and 70 °C, respectively. All enzyme activity was destroyed after exposured in 100 °C for 10 min. The peroxidase did not exhibit HIV-1 reverse transcriptase inhibitory activity and antifungal activity. The stability against high temperature and extreme pH supported that the enzyme could be a potential peroxidase source for special industrial applications.
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