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- W2900281652 abstract "The thermostable esterase Aaeo1 displays a low expression level and forms a great amount of inclusion bodies in E. coli. Herein, a split-GFP system was established in which the fluorescence intensity exhibited a good linear correlation with the soluble protein expression level and the esterase activity. In the primary high-throughput screening, the mutant library was screened by flow cytometry via detection of a split-GFP reporter. Then, through a secondary screening against esterase activity, two mutants with improved soluble expression and catalytic activity were obtained. The soluble expression of the mutant enzymes in E. coli was improved by 2-fold. The kcat/Km values of the mutant enzymes were 2-fold higher than that of the parent. We explored the relationship between the amino acid mutations in the two mutants and the enzyme activity. The enzyme activity of mutant I51V-E170D was 4.5 times higher than that of the parent." @default.
- W2900281652 created "2018-11-16" @default.
- W2900281652 creator A5000831108 @default.
- W2900281652 creator A5004381930 @default.
- W2900281652 creator A5034094966 @default.
- W2900281652 date "2018-11-09" @default.
- W2900281652 modified "2023-10-14" @default.
- W2900281652 title "Improved Soluble Expression and Catalytic Activity of a Thermostable Esterase Using a High-Throughput Screening System Based on a Split-GFP Assembly" @default.
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- W2900281652 doi "https://doi.org/10.1021/acs.jafc.8b04646" @default.
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