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S. fradiae exhibited the highest acetanilide p-hydroxylation activity among the Streptomyces spp. screened. Studies with inhibitors (metyrapone, 2,6-dichloroindophenol, a,a’’-dipyridyl, o-phenanthroline) and an absorption peak after CO treatment suggested that S. fradiae hydroxylase activity was due to cytochrome p-450. This hydroxylase activity was increased to ten times in the cell extract containing 0.5mM sodium azide. Furthermore, the sedimentary activity in 105,00O X g centrifugal forces and solubilization of the activity with Triton-X 100 implied that this enzyme was membrane bound monooxygenase. pH Optimum of the enzyme was 6.5 in membrane bound state.
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