Expression, purification, and characterization of a 2,3-dihydroxybiphenyl-1,2-dioxygenase from Bacillus sp JF8 in Escherichia coli
文献类型： 外文期刊
作者： Bian, Lin 1 ; Shuai, Jian-Jun 1 ; Xiong, Fei 3 ; Peng, Ri-He 2 ; Yao, Quan-Hong 2 ; Xiong, Ai-Sheng 1 ;
作者机构： 1.Nanjing Agr Univ, Coll Hort, Nanjing 210095, Jiangsu, Peoples R China
2.Shanghai Acad Agr Sci, Biotechnol Res Inst, Shanghai 201106, Peoples R China
3.Yangzhou Univ, Coll Biosci & Biotechnol, Yangzhou 225009, Peoples R China
关键词： Biodegradation;BsbphCI gene;2,3-Dihydroxybiphenyl-1,2-dioxygenase;2,3-Dihydroxybiphenyl;HPLC
期刊名称：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS （ 影响因子：3.575； 五年影响因子：3.381 ）
ISSN： 0006-291X
年卷期： 2012 年 419 卷 2 期
页码：
收录情况： SCI
摘要： 2,3-Dihydroxybiphenyl-1,2-dioxygenase plays an important role in the degradation of polychlorinated biphenyls. The gene (BsbphCI) encoding a 2,3-DHBP dioxygenase from Bacillus sp. JF8 is 960 bp. We synthesized a 960 bp BsbphCI gene encoding a 2,3-DHBP dioxygenase derived from Bacillus sp. JF8 and expressed it in Escherichia coli. The recombinant protein was about 36 kDa, confirmed by SDS-PAGE. The concentration of the purified protein was about 1.8 mg/mL. With 2,3-DHBP as a substrate, the optimal temperature for enzyme activity at pH 8.5 was 50 degrees C. The optimal pH for the 2,3-DHBP dioxygenase was 8.5. The enzyme retained 33% activity after heating at 60 degrees C for 60 min. We found that Cu2+, K+, Zn2+, Mg2+, Ni2+, CO2+, and Cd2+ activated the enzyme. However, Ca2+, Fe2+, Li+, and Cr3+ inhibited it. Enzyme activity was reduced by exposure to H2O2, SDS, and KI. The results of HPLC indicated that the transgenic E. coli strain with the BstvhCI gene degraded 2,3-DHBP more quickly than the wild type strain. (C) 2012 Elsevier Inc. All rights reserved.
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