Oleic acid based experimental evolution of Bacillus megaterium yielding an enhanced P450 BM3 variant.

ABSTRACT:

Background

Unlike most other P450 cytochrome monooxygenases, CYP102A1 from Bacillus megaterium (BM3) is both soluble and fused to its redox partner forming a single polypeptide chain. Like other monooxygenases, it can catalyze the insertion of oxygen unto the carbon-hydrogen bond which can result in a wide variety of commercially relevant products for pharmaceutical and fine chemical industries. However, the instability of the enzyme holds back the implementation of a BM3-based biocatalytic industrial processes due to the important enzyme cost it would prompt.

Results

In this work, we sought to enhance BM3's total specific product output by using experimental evolution, an approach not yet reported to improve this enzyme. By exploiting B. megaterium's own oleic acid metaboli

SUBMITTER: Vincent T 

PROVIDER: S-EPMC9281120 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature