Surface display of heme- and diflavin-containing cytochrome P450 BM3 in Escherichia coli: a whole cell biocatalyst for oxidation

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dc.contributor.authorS K Yim-
dc.contributor.authorD H Kim-
dc.contributor.authorHeung Chae Jung-
dc.contributor.authorJae Gu Pan-
dc.contributor.authorH S Kang-
dc.contributor.authorT Ahn-
dc.contributor.authorC H Yun-
dc.date.accessioned2017-04-19T09:19:28Z-
dc.date.available2017-04-19T09:19:28Z-
dc.date.issued2010-
dc.identifier.issn1017-7825-
dc.identifier.uri10.4014/jmb.0910.10043ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9679-
dc.description.abstractCytochrome P450 enzymes (P450s) are involved in the synthesis of a wide variety of valuable products and in the degradation of numerous toxic compounds. The P450 BM3 (CYP102A1) from Bacillus megaterium was the first P450 discovered to be fused to its redox partner, a mammalian-like diflavin reductase. Here, we report the development of a whole-cell biocatalyst using ice-nucleation protein (Inp) from Pseudomonas syringae to display a heme- and diflavin-containing oxidoreductase, P450 BM3 (a single, 119-kDa polypeptide with domains of both an oxygenase and a reductase) on the surface of Escherichia coli. The surface localization and functionality of the fusion protein containing P450 BM3 were verified by flow cytometry and measurement of enzymatic activities. The results of this study comprise the first report of microbial cell-surface display of a heme- and diflavin-containing enzyme. This system should allow us to select and develop oxidoreductases containing heme and/or flavins into practically useful whole-cell biocatalysts for extensive biotechnological applications, including selective synthesis of new chemicals and pharmaceuticals, bioconversion, bioremediation, live vaccine development, and biochip development.-
dc.publisherKorea Soc-Assoc-Inst-
dc.titleSurface display of heme- and diflavin-containing cytochrome P450 BM3 in Escherichia coli: a whole cell biocatalyst for oxidation-
dc.title.alternativeSurface display of heme- and diflavin-containing cytochrome P450 BM3 in Escherichia coli: a whole cell biocatalyst for oxidation-
dc.typeArticle-
dc.citation.titleJournal of Microbiology and Biotechnology-
dc.citation.number4-
dc.citation.endPage717-
dc.citation.startPage712-
dc.citation.volume20-
dc.contributor.affiliatedAuthorHeung Chae Jung-
dc.contributor.affiliatedAuthorJae Gu Pan-
dc.contributor.alternativeName임성근-
dc.contributor.alternativeName김동현-
dc.contributor.alternativeName정흥채-
dc.contributor.alternativeName반재구-
dc.contributor.alternativeName강형식-
dc.contributor.alternativeName안태호-
dc.contributor.alternativeName윤철호-
dc.identifier.bibliographicCitationJournal of Microbiology and Biotechnology, vol. 20, no. 4, pp. 712-717-
dc.identifier.doi10.4014/jmb.0910.10043-
dc.subject.keywordOxidation-
dc.subject.keywordP450 BM3-
dc.subject.keywordSurface display-
dc.subject.keywordWhole-cell biocatalyst-
dc.subject.localoxidation-
dc.subject.localOxidation-
dc.subject.localP450 BM3-
dc.subject.localSurface display-
dc.subject.localsurface display-
dc.subject.localWhole-cell biocatalyst-
dc.subject.localwhole-cell biocatalyst-
dc.description.journalClassY-
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Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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