Purification and characterization of an aflatoxin degradation enzyme from Pleurotus ostreatus

被引:159
作者
Motomura, M
Toyomasu, T
Mizuno, K
Shinozawa, T [1 ]
机构
[1] Gunma Univ, Fac Engn, Dept Biol & Chem Engn, Kiryu, Gumma 3768515, Japan
[2] Mushroon Res Inst Japan, Kiryu, Gumma 3760051, Japan
关键词
aflatoxin degradation; Pleurotus ostreatus; enzyme purification; lactone cleavage;
D O I
10.1078/0944-5013-00199
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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 SIDS-PAGE. Optimum activities were found in the pH range between 4.0 and 5.0 and at 25 degreesC. Also, degradation activity of several dyes in the presence of H2O2 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.
引用
收藏
页码:237 / 242
页数:6
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