Detoxification of Aflatoxin B1 Contaminated Maize Using Human CYP3A4

被引:14
|
作者
Yamada, Marie [1 ]
Hatsuta, Koji [1 ]
Niikawa, Mayuko [1 ]
Imaishi, Hiromasa [1 ]
机构
[1] Kobe Univ, Biosignal Res Ctr, Div Signal Responses, Nada Ku, Kobe, Hyogo 6578501, Japan
基金
日本学术振兴会;
关键词
Aflatoxin B-1; cytochrome P450; CYP3A4; detoxification; CYTOCHROME-P450; INHIBITION; METABOLISM; ACTIVATION; MORPHOLOGY; PROTEINS; BINDING; ACID;
D O I
10.4014/jmb.2003.03032
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Aflatoxin B1 (AFB1) is a mycotoxin produced by Aspergillus flavus (A. flavus). AFB1 is reported to have high thermal stability and is not decomposed by heat treatment during food processing. Therefore, in this study, knowing that AFB1 is metabolized by cytochrome P450 (CYP), our aim was to develop a method to detoxify A. flavus-contaminated maize, under normal temperature and pressure, using Escherichia coli expressing human CYP3A4. First, the metabolic activity of AFB1 by recombinant human CYP3A4 was evaluated. As a result, we confirmed that recombinant human CYP3A4 metabolizes 98% of AFB1. Next, we found that aflatoxin Q1, a metabolite of AFB1 was no longer mutagenic. Furthermore, we revealed that about 50% of the AFB1 metabolic activity can be maintained for 3 months when E. coli expressing human CYP3A4 is freeze-dried in the presence of trehalose. Finally, we found that 80% of AFB1 in A. flavus-contaminated maize was metabolized by E. coli expressing human CYP3A4 in the presence of surfactant triton X-405 at a final concentration of 10% (v/v). From these results, we conclude that AFB1 in A. flavus-contaminated maize can be detoxified under normal temperature and pressure by using E. coli expressing human CYP3A4.
引用
收藏
页码:1207 / 1213
页数:7
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