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• W3101418990 abstract "Abstract Baeyer‐Villiger monooxygenases (BVMOs) are remarkable biocatalysts for the Baeyer‐Villiger oxidation of ketones to generate esters or lactones. The regioselectivity of BVMOs is essential for determining the ratio of the two regioisomeric products (“normal” and “abnormal”) when catalyzing asymmetric ketone substrates. Starting from a known normal‐preferring BVMO sequence from Pseudomonas putida KT2440 ( Pp BVMO), a novel BVMO from Gordonia sihwensis ( Gs BVMO) with higher normal regioselectivity (up to 97/3) was identified. Furthermore, protein engineering increased the specificity constant ( k cat / K M ) 8.9‐fold to 484 s −1 mM −1 for 10‐ketostearic acid derived from oleic acid. Consequently, by using the variant Gs BVMO C308L as an efficient biocatalyst, 10‐ketostearic acid was efficiently transformed into 9‐(nonanoyloxy)nonanoic acid, with a space‐time yield of 60.5 g L −1 d −1 . This study showed that the mutant with higher regioselectivity and catalytic efficiency could be applied to prepare medium‐chain ω‐hydroxy fatty acids through biotransformation of long‐chain aliphatic keto acids derived from renewable plant oils." @default.
• W3101418990 created "2020-11-23" @default.
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• W3101418990 date "2020-12-14" @default.
• W3101418990 modified "2023-10-18" @default.
• W3101418990 title "Discovery and Engineering of a Novel Baeyer‐Villiger Monooxygenase with High Normal Regioselectivity" @default.
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• W3101418990 doi "https://doi.org/10.1002/cbic.202000478" @default.
• W3101418990 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33205522" @default.
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