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This paper describes the measurement and analysis of  in vivo  activity and stability of cyclohexanone monooxygenase from  Acinetobacter  sp. NCIMB 9871 (CHMO), a model Baeyer–Villiger monooxygenase, in the recombinant host  Escherichia coli . This enzyme was often described as poorly stable  in vitro , and has recently been found to deactivate rapidly in the absence of its essential cofactors and antioxidants. Its stability  in vivo  was scarcely studied, so far. Under conditions common for the overexpression of CHMO we investigated the ability of the host to support these properties using metabolomics. Our results showed that  E. coli  failed to provide the intracellular levels of cofactors required to functionally stabilize the enzyme, although the biocatalyst was produced in high concentration, and was invariably detected after protein synthesis had stopped. We thus infer that biotechnological applications of CHMO with this host relied on a residual activity of approximately 5-10%. Other microorganisms might offer a more efficient solution for recombinant production of CHMO and related enzymes.

Escherichia coli Fails to Efficiently Maintain the Activity of an Important Flavin Monooxygenase in Recombinant Overexpression