文章基本信息

标题：Enzymatic Interconversion of Aflatoxin B1 and Aflatoxicol by Rhizopus sp.
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作者：MITSUO NAKAZATO ; SATOSHI MOROZUMI ; KAZUO SAITO 等
期刊名称：Journal of Health Science
印刷版ISSN：1344-9702
电子版ISSN：1347-5207
出版年度：1991
卷号：37
期号：4
页码：288-295
DOI：10.1248/jhs1956.37.288
出版社：The Pharmaceutical Society of Japan
摘要：We found that an enzyme extracted from mycelia of Rhizopus sp. had potent interconversion activities of aflatoxin B₁ (AF B₁) and aflatoxicol A (AFL-A). The enzyme was suggested to be an NADP-dependent oxidoreductase, since both the oxidative conversion of AFL-A to AF B₁ and the reductive conversion of AF B₁ to AFL-A were found with completely the same patterns in fractions obtained by gel permeation and ion exchange chromatography. The enzyme had an apparent molecular weight of 40000 in gel permeation chromatography on Sephacryl S-200HR. The optimum pH for conversion of AF B₁ to AFL-A was around 6.0 to 7.0, while that of AFL-A to AF B₁ was around 7.5 to 9.0, at 35°C. The optimum temperature was 35°C for both conversions of AF B₁ to AFL-A and of AFL-A to AF B₁. Furthermore, only AFL-A, the (S)-isomer was produced from AF B₁ by catalysis by NADP-dependent oxidoreductase. However, we were unable to purify the enzyme to homogeneity by ammonium sulfate saturation, by chromatography on Sephacryl S-200HR, DEAE-Sepharose Fast Flow and 2', 5'ADP-Sepharose 4B.
关键词：mycotoxin;aflatoxin B1;aflatoxicol A;aflatoxicol B;fungus;Rhizopus sp.;enzyme;oxidoreductase;coenzyme;NADP