کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
17504 42673 2011 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Screening of bacterial cytochrome P450s responsible for regiospecific hydroxylation of (iso)flavonoids
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Screening of bacterial cytochrome P450s responsible for regiospecific hydroxylation of (iso)flavonoids
چکیده انگلیسی

Screening of cytochrome P450 monoxygenases responsible for the regiospecific hydroxylation of flavones, isoflavones and chalcones was attempted using a P450 library constructed from Streptomyces avermitilis MA4680, Bacillus and Nocardia farcinica IFM10152 strains. As electron transfer redox partners with the P450s in Escherichia coli system, putidaredoxin reductase (PdR) and putidaredoxin (Pdx) from Pseudomonas putida were used. Among the 50 soluble P450s in the library screened, three cytochrome P450s, i.e. CYP107Y1, CYP125A2 and CYP107P2 from S. avermitilis MA4680 showed good hydroxylation activities towards flavones and isoflavones. However, low product yields prevented us from identifying complete structure of the products. By using S. avermitilis MA4680 as their expression host, further analysis identified that CYP107Y1(SAV2377), CYP125A2(SAV5841) and CYP107P2(SAV4539) showed good regiospecific hydroxylation activities towards genistein (4′,5,7-trihydroxyisoflavone), chrysin (5,7-dihydroxyisoflavone) and apigenin (4′,5,7-dihydroxyisoflavone) to produce 3′,4′,5,7,-tetrahydroxyisoflavone, B-ring hydroxylated 5,7-dihydroxyflavone and 3′,4′,5,7,-tetrahydroxyflavone, respectively. Analyses of the reaction products were performed using HPLC, ESI-MS–MS and GC–MS and 1H NMR.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Enzyme and Microbial Technology - Volume 48, Issues 4–5, 7 April 2011, Pages 386–392
نویسندگان
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