Purification and characterization of an aflatoxin degradation enzyme from Pleurotus ostreatus

Nineteen fungi were tested for their ability to degrade aflatoxin B 1 (AFB 1). An extracellular enzyme from the edible mushroom Pleurotus ostreatus showed afaltoxin-degradation activity detected by thin-layer chromatography (TLC). An enzyme with this activity was purified by two chromatographies on...

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Veröffentlicht in:Microbiological research 2003-01, Vol.158 (3), p.237-242
Hauptverfasser: Motomura, Marisa, Toyomasu, Tetsuo, Mizuno, Keiko, Shinozawa, Takao
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Sprache:eng
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Zusammenfassung:Nineteen fungi were tested for their ability to degrade aflatoxin B 1 (AFB 1). An extracellular enzyme from the edible mushroom Pleurotus ostreatus showed afaltoxin-degradation activity detected by thin-layer chromatography (TLC). An enzyme with this activity was purified by two chromatographies on DEAE-Sepharose and Phenyl-Sepharose. The apparent molecular mass of the purified enzyme was estimated to be 90 kDa by SDS-PAGE. Optimum activities were found in the pH range between 4.0 and 5.0 and at 25°C. Also, degradation activity of several dyes in the presence of H 2O 2 was tested, resulting in the detection of bromophenol blue-decolorizing activity. Based on these data, we suggest this enzyme is a novel enzyme with aflatoxin-degradation activity. Fluorescence measurements suggest that the enzyme cleaves the lactone ring of aflatoxin.
ISSN:0944-5013
1618-0623
DOI:10.1078/0944-5013-00199