원문정보
초록
영어
Cytochrome P450s act on the inactive carbon-hydrogen bonds of alkanes, fatty acids, terpenes, and steroids; and some exhibit high regio and stereoselective monooxygenation activity. And cytochrome P450s are expected to be potential catalysts for fine chemical synthesis. Regiospecific hydroxylation of isoflavone using cells of Bacteria, actinomyce was examined. Recent researches reported hydroxylated isoflavones have an effect on the anticancer, antitumor, and antioxidant. Daidzein, the major soy isoflavone was finally hydroxylated by whole cell reaction with Streptomyces avermitilis MA4680 and Nocardia farcinica IFM10152.
The major hydroxylated products of daidzein were 7,3’,4’-trihydroxyisoflavone, 6,7,4’-
trihydroxyisoflavone and 7,8,4’-trihydroxyisoflavone which were mono-hydroxylated at ortho position of hydroxy group of daidzein. Also we identified P450 monooxygenases involved in monohydroxylation of daidzein and expressed in E. coli. P450s need redox partner for hydroxylation to transfer electrons to the heme domain of P450 and activate the hydroxylation step of the substrate-heme domain complex. We constructed P450s and redox partners which matched best in E. coli . The hydroxylated products were determined using high performance liquid chromatograph (HPLC), gas chrmomatograph / mass spectrometry (GC/MS)
Acknowledgement : This research was supported by a grant from the National Research Laboratory Program of the Korea Science and Engineering Foundation.(Grant No. ROA-2007-000-10007-0)