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   <subfield code="a">Enzymatic study on acetanilide p -hydroxylase in Streptomyces fradiae</subfield>
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   <subfield code="a">S. fradiae exhibited the highest acetanilidep-hydroxylation activity among theStreptomyces spp. Studies with inhibitors (metyrapone, 2,6-dichloroindophenol, α,α′-dipyridyl,o-phenanthroline) and an absorption peak after CO treatment suggested thatS. fradiae hydroxylase activity was due to cytochrome p-450. This hydroxylase activity was increased to ten times in the cell extract containing 0.5 mM sodium azide. Further-more, the sedimentary activity in 105,000×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.</subfield>
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