Abstract
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.
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