Functional expression in Bacillus subtilis of mammalian NADPH-cytochrome P450 oxidoreductase and its spore-display

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dc.contributor.authorSung-Kun Yim-
dc.contributor.authorHeung Chae Jung-
dc.contributor.authorC H Yun-
dc.contributor.authorJae Gu Pan-
dc.date.accessioned2017-04-19T09:12:05Z-
dc.date.available2017-04-19T09:12:05Z-
dc.date.issued2009-
dc.identifier.issn1046-5928-
dc.identifier.uri10.1016/j.pep.2008.07.004ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8682-
dc.description.abstractThe technology for over-expressing NADPH-cytochrome P450 reductase (CPR), a diflavin-containing enzyme, offers the opportunity to develop enzymatic systems for environmental detoxication and bioconversions of drugs, pesticides and fine chemicals. In this study, Bacillus subtilis was chosen to express rat CPR (rCPR) because of its capacities for high protein production and spore formation. rCPR was expressed in B. subtilis DB104 under the transcriptional control of an IPTG-inducible fusion promoter of PgroE and Ptac. The expressed rCPR was released into the culture medium after sporulation by autolysis of the host cell. It was associated with and displayed on the spore surfaces; this was confirmed by measuring rCPR activity in purified spores and analyzing its accessibility to anti-rCPR antibodies using flow cytometry. The spore-displayed rCPR was able to reduce cytochrome c and ferricyanide, and also assisted in the O-deethylation of 7-ethoxyresorufin and 7-ethoxy-4-trifluoromethylcoumarin (EFC) by human cytochrome P450 1A2, indicating that it was functionally active. Spore surface display of rCPR in B. subtilis appears to be useful for preparing cytochrome P450-related enzymes, and spore biocatalysts of rCPR are likely to have wide biotechnological applications.-
dc.publisherElsevier-
dc.titleFunctional expression in Bacillus subtilis of mammalian NADPH-cytochrome P450 oxidoreductase and its spore-display-
dc.title.alternativeFunctional expression in Bacillus subtilis of mammalian NADPH-cytochrome P450 oxidoreductase and its spore-display-
dc.typeArticle-
dc.citation.titleProtein Expression and Purification-
dc.citation.number1-
dc.citation.endPage11-
dc.citation.startPage5-
dc.citation.volume63-
dc.contributor.affiliatedAuthorHeung Chae Jung-
dc.contributor.affiliatedAuthorJae Gu Pan-
dc.contributor.alternativeName임성근-
dc.contributor.alternativeName정흥채-
dc.contributor.alternativeName윤철호-
dc.contributor.alternativeName반재구-
dc.identifier.bibliographicCitationProtein Expression and Purification, vol. 63, no. 1, pp. 5-11-
dc.identifier.doi10.1016/j.pep.2008.07.004-
dc.subject.keywordbacillus expression-
dc.subject.keywordCPR-
dc.subject.keywordNADPH-cytochrome P450 reductase-
dc.subject.keywordspore-display-
dc.subject.keywordwhole-cell biocatalyst-
dc.subject.localbacillus expression-
dc.subject.localCPR-
dc.subject.localNADPH-cytochrome P450 reductase-
dc.subject.localspore-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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