A new paradigm for biohydroxylation by Beauveria bassiana ATCC 7159

The biohydroxylation of a series of amides and related amino, keto and hydr ocarbon substrates by the fungal biocatalyst Beauveria bassiana ATCC 7159 h as been examined. The product distributions, together with data obtained fr om selective inhibition experiments using the cyt.P-450 inhibitors isosafro le, 1-aminobenzotriazole and phenylacetylene, suggest that B. bassiana cont ains a range of hydroxylase enzymes with different substrate specificities. A paradigm is presented for the interpretation of the results of microbial hydroxylation and for the application of existing active site models for B . bassiana. (C) 1999 Elsevier Science Ltd. All rights reserved.