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- W3154175065 abstract "Abstract Cyclohexanone monooxygenase (CHMO), a member of the Baeyer–Villiger monooxygenase family, is a versatile biocatalyst that efficiently catalyzes the conversion of cyclic ketones to lactones. In this study, an Acidovorax‐ derived CHMO gene was expressed in Pseudomonas taiwanensis VLB120. Upon purification, the enzyme was characterized in vitro and shown to feature a broad substrate spectrum and up to 100% conversion in 6 h. Furthermore, we determined and compared the cyclohexanone conversion kinetics for different CHMO‐biocatalyst formats, that is, isolated enzyme, suspended whole cells, and biofilms, the latter two based on recombinant CHMO‐containing P. taiwanensis VLB120. Biofilms showed less favorable values for K S (9.3‐fold higher) and k cat (4.8‐fold lower) compared with corresponding K M and k cat values of isolated CHMO, but a favorable K I for cyclohexanone (5.3‐fold higher). The unfavorable K S and k cat values are related to mass transfer‐ and possibly heterogeneity issues and deserve further investigation and engineering, to exploit the high potential of biofilms regarding process stability. Suspended cells showed only 1.8‐fold higher K S , but 1.3‐ and 4.2‐fold higher k cat and K I values than isolated CHMO. This together with the efficient NADPH regeneration via glucose metabolism makes this format highly promising from a kinetics perspective." @default.
- W3154175065 created "2021-04-26" @default.
- W3154175065 creator A5029141813 @default.
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- W3154175065 creator A5063934346 @default.
- W3154175065 creator A5065176224 @default.
- W3154175065 date "2021-05-05" @default.
- W3154175065 modified "2023-10-17" @default.
- W3154175065 title "Characterization of different biocatalyst formats for BVMO‐catalyzed cyclohexanone oxidation" @default.
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- W3154175065 doi "https://doi.org/10.1002/bit.27791" @default.
- W3154175065 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33844297" @default.
- W3154175065 hasPublicationYear "2021" @default.
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