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KMID : 1094720080130010069
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Biotechnology and Bioprocess Engineering
2008 Volume.13 No. 1 p.69 ~ p.76
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Construction and characterization of a recombinant whole-cell biocatalyst of Escherichia coli expressing styrene monooxygenase under the control of arabinose promoter
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Bae Jong-Wan
Shin Seung-Hee
Raj S. Mohan
Lee Song-Eun
Lee Sun-Gu
Jeong Yong-Joo
Park Sung-Hoon
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Abstract
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A recombinant Escherichia coli (pBAB1) containing styrene monooxygenase (SMO) was developed for the conversion of styrene to enantiopure (S)-styrene oxide that is an important chiral building block in organic synthesis. The styAB genes encoding SMO was cloned into a multicopy plasmid under the tightly regulated promoter of bacterial l-arabinose operon which is inducible by l-arabinose. The recombinant showed that expression level of StyA protein and whole-cell SMO activities were varied depending on the concentration of the inducer l-arabinose. The maximum SMO activity was 108 U/g cdw when the cells were induced with 0.2% l-arabinose. SDS-PAGE and Western blot analyses indicated that whole-cell SMO activity was strongly correlated with the expression level of StyA protein. Organic-aqueous two-phase experiment could yield 50 mM enantiopure (S)-styrene oxide in organic phase in 18 h, but the recombinant SMO activity was unstable during the reaction. The expression of styAB under the control of l-arabinose promoter was significantly repressed in the presence of glucose.
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KEYWORD
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(S)-styrene oxide, styrene monooxygenase, arabinose promoter, pBAD, whole-cell biocatalyst
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