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KMID : 1034820120080040375
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Molecular & Cellular Toxicology
2012 Volume.8 No. 4 p.375 ~ p.382
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Expression and characterization of a recombinant 2,3-dihydroxybiphenyl-1,2-dioxygenase from Pseudomonas
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Xiong Fei
Shuai Jian-Jun
Jin Xiao-Fen
Zhang Jian
Sun Jing
Peng Ri-He
Yao Quan-Hong
Xiong Ai-Sheng
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Abstract
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The 2, 3-dihydroxybiphenyl-1,2-dioxygenase, which can degrade the 2,3-dihydroxybiphenyl, was encoded by a synthesized PsbphCI gene. The PsbphCI gene was transformed into Escherichia coli and the encoding protein purified, had a molecular mass of ∼32 kDa as determined by SDS-PAGE. The optimum pH for the purified enzyme at 20°C was 9.0, and the optimal temperature at pH 8.0 was 30°C. Subsequently, the PsbphCI gene was transformed into Pseudomonas putida sp. to verify the degradation of 2,3-dihydroxybiphenyl by HPLC. The transgenic EG11 strain degraded 65.20% of the 2,3-DHBP after 2 minutes at 30°C, while the wild-type EG11 strain degraded only 37.75%. This study provides guidance for the cultivation of bioengineered biphenyl/PCBs-degrading bacteria which can be applied to the biodegradation of environmental biphenyl/PCBs contamination.
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KEYWORD
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PsbphCI gene, 2,3-dihydroxybiphenyl-1,2-dioxygenase, Synthesized gene, 2,3-dihydroxybiphenyl, HPLC
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