期刊
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
卷 66, 期 4, 页码 1429-1434出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.66.4.1429-1434.2000
关键词
-
A flavin reductase, which is naturally part of the ribonucleotide reductase complex of Escherichia coli, acted in cell extracts of recombinant E, coli strains under aerobic and anaerobic conditions as an azo reductase. The transfer of the recombinant plasmid, which resulted in the constitutive expression of high levels of activity of the flavin reductase, increased the reduction rate for different industrially relevant sulfonated azo dyes in vitro almost 100-fold. The flavin reductase gene (fre) was transferred to Sphingomonas sp. strain BN6, a bacterial strain able to degrade naphthalenesulfonates under aerobic conditions. The flavin reductase was also synthesized in significant amounts in the Sphingomonas strain. The reduction rates for the sulfonated azo compound amaranth were compared for whole cells and cell extracts from both recombinant strains, E, coli, and wild-type Sphingomonas sp. strain BN6. The whole cells showed less than 2% of the specific activities found with cell extracts. These results suggested that the cytoplasmic anaerobic azo reductases, which have been described repeatedly in in vitro systems, are presumably Ravin reductases and that in vivo they have insignificant importance in the reduction of sulfonated azo compounds.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据