Enhancing the Activity of a Dietzia sp. D5 Baeyer-Villiger Monooxygenase towards Cyclohexanone by Saturation Mutagenesis
A recombinant Baeyer-Villiger monooxygenase, BVMO4 from Dietzia sp. D5 has been previously reported. The enzyme exhibited good thermostability and was active with a wide range of cyclic ketone substrates but catalysed poorly the conversion of cyclohexanone to caprolactone. The present work focuses on protein engineering of BVMO4 to improve the conversion of cyclohexanone. Thus, a structural model
