Institute of Microbial Technology, Jinan University, Guangzhou City, Guangdong Province 510632, China.
Microbiol Res. 2011 Sep 20;166(6):475-83. doi: 10.1016/j.micres.2010.09.002. Epub 2011 Jan 15.
Armillariella tabescens, a Chinese edible and medicinal fungus, whose multienzyme exist ability of AFB(1)-converting, and ADTZ (aflatoxin-detoxizyme) had previously purified from the A. tabescens multienzyme monitored by AFB(1) conversion(.) However, the enzyme now confirmed an oxidase and renamed aflatoxin-oxidase (AFO). In this paper, AFO was purified by an economical and practical three-step procedure monitored by AFB(1) conversion. And ESI-MS/MS analysis was done for identification of AFO. The following database searching (Protein Blast on NCBI) results did not show any homologous oxidase protein, which implied that AFO was mostly a new oxidase differing from other reported aflatoxin-converting enzymes such as fungal laccase and horse radish peroxidase. HPTLC analysis of the purified AFO activity suggested that the enzyme reacted at the bisfuran ring of AFB(1) which was the key toxic structure. Therefore, all these investigations implied a new choice for biodegradation of aflatoxin in foods and feeds with the practical application of AFO.
双孢蘑菇，一种中国产的食用和药用真菌，其多酶存在的能力的 AFB(1)-转化，和 ADTZ (黄曲霉毒素解毒酶) 已从 A. tabescens 多酶监测 AFB(1) 转换之前被纯化。然而，该酶现在被确认为氧化酶，并更名为黄曲霉毒素氧化酶 (AFO)。在本文中，通过 AFB(1) 转化监测的经济实用的三步程序对 AFO 进行了纯化。并进行了 ESI-MS/MS 分析以鉴定 AFO。以下数据库搜索 (NCBI 上的蛋白质 Blast) 结果未显示任何同源氧化酶蛋白，这表明 AFO 主要是一种新的氧化酶，与其他报道的黄曲霉毒素转化酶如真菌漆酶和辣根过氧化物酶不同。纯化 AFO 活性的 HPTLC 分析表明，该酶在 AFB(1) 的双呋喃环上反应，这是关键的毒性结构。因此，所有这些研究都为食品和饲料中黄曲霉毒素的生物降解提供了新的选择，具有 AFO 的实际应用。
