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Computational-Aided Mutagenesis of Lipase CRL1 with Promoted Stability and Activity for Biosynthesis of Vitamin E Succinate
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DOI：10.1021/acs.jafc.6c02908.png)
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Abstract
En 中文
Vitamin E succinate (VES) is a particularly potent form of vitamin E derivatives in daily supplements. The promising biocatalyst crude lipase CRL (Candida rugosa lipase) could produce vitamin E succinate but suffers from low yield due to limited thermostability. This study integrated computational-aided virtual mutagenesis and combinatorial mutations of lipase CRL1. A combinatorial variant 6M (K85P/V86W/T108V/T132W/F344I/V454L) synchronously enhanced thermostability and pH stability, and half-lives were 322.7 min (60 °C) and 201.2 min (70 °C), representing a 6.35-fold and 7.31-fold increase compared to WT, respectively. 6M’s lipase activity was 2 times that of WT, and the catalytic efficiency (kcat/Km) showed a 6.8-fold improvement over that of WT. Mutant 6M could generate vitamin E succinate with an improved yield of 77.8% (60 °C, 12 h). The synergistically functional modifications of the lipase pave the way for the mutated lipase to become a highly promising and robust biocatalyst for industrial applications.
Keywords:
Genetics
Nutrition
Organic compounds
Peptides and proteins
Thermal stability
vitamin E succinate
lipase CRL1
thermal stability
computational-aided mutagenesis
molecular dynamics simulation
Journal
IF:
6.2
Papers:
4.5W
Citations:
15.3W
Organization
Cited Papers