Journal
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
Volume 59, Issue 4, Pages 248-253Publisher
ELSEVIER
DOI: 10.1016/j.molcatb.2008.07.005
Keywords
CYP107H1; Daidzein; Redox partner; Biocatalyst; Hydroxylation
Funding
- Korea Health 21 RD Project
- Ministry of Health Welfare
- Ministry of Education, Republic of Korea [A05-0572-A11101-06A2-00020B]
- Korea Ministry of Science and Technology, South Korea [R0A-2007-000-10007-0]
- National Research Foundation of Korea [R0A-2007-000-10007-0] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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CYP107H1, from Bacillus subtilis 168 known as fatty acid hydroxylase, showed the ortho-specific hydroxylation activity to daidzein, when coupled to the putidaredoxin reductase (camA) and putidaredoxin (camB) from Pseudomonas putida as the redox partners. The electron transfer system of the three proteins was constructed in Escherichia coli BL21 (DE3) system using the two plasmids containing different selection markers. The daidzein hydroxylation was demonstrated with recombinant whole cell and in vitro system using the artificial redox partner for electron transfer. The identification of the hydroxylation reaction yielding 7,3 ',4 '-trihydroxyisoflavone was elucidated using gas chromatography mass spectrometry (GC-MS). This oxidizing activity of CYP107H1 towards daidzein represents the new hydroxylation of aromatic compound as substrate. (C) 2008 Elsevier B.V. All rights reserved.
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