4.6 Article

Temperature and solvent exposure response of three fatty acid peroxygenase enzymes for application in industrial enzyme processes

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出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2021.07.052

关键词

Hydrogen peroxide; Cytochrome P450 (CYP450); Peroxygenases; Biocatalysis; OleT; CYP152K6

资金

  1. National Science Foundation Emerging Frontiers in Research and Innovation [1332341]

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Research has shown that the fatty acid peroxygenase CYP152K6 from Bacillus methanolicus exhibits higher stability at high temperatures compared to other CYP152 enzymes, providing a significant advantage for industrial applications.
Free fatty acids (FFAs) are a useful feedstock for a range of industrial chemical synthesis applications. However, efficiently converting FFAs to molecules for biofuel and other high-value chemicals requires more efficient and cost-effective catalysts. Cytochrome P450 fatty acid peroxygenases (CYP152) have a unique chemistry that allows use of the peroxide shunt pathway for biochemical conversion of FFAs. Known CYP152s are heat labile, however, requiring characterization of more thermotolerant versions for use in industrial applications. A fatty acid peroxygenase from Bacillus methanolicus (CYP152K6) was shown here to have a higher optimal reaction temperature than OleT (CYP152L1). CYP152K6 was stable up to 50 degrees C and showed great stability in 3% acetone and dimethylformamide. Stability in solvents helps the enzyme's substrates remain soluble in solution for more efficient catalysis, and heat stability allows enzymes to remain active longer during industrial processes. (C) 2021 Elsevier Inc. All rights reserved.

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