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- W2806811675 abstract "The aminotransferase ARO8 was proved to play an efficient role in conversion of l-methionine into methionol via the Ehrlich pathway in Saccharomyces cerevisiae in our previous work. In this work, the reversible transamination activity of ARO8 for conversion of α-keto-γ-(methylthio) butyric acid (KMBA) into l-methionine was confirmed in vitro. ARO8 was cloned from S. cerevisiae S288c and overexpressed in Escherichia coli BL21. A 2-fold higher aminotransferase activity was detected in the recombinant strain ARO8-BL21, and ARO8 was detected in the supernatant of ARO8-BL21 lysate with IPTG induction by SDS-PAGE analysis. The recombinant ARO8 was then purified and used for transforming KMBA into l-methionine. An approximately 100% conversion rate of KMBA into l-methionine was achieved by optimized enzymatic reaction catalyzed by ARO8. This work fulfilled l-methionine biosynthesis catalyzed by the aminotransferase ARO8 using glutamate and KMBA, which provided a novel method for l-methionine production by enzymatic catalysis with the potential application prospect in industry." @default.
- W2806811675 created "2018-06-13" @default.
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- W2806811675 date "2018-05-28" @default.
- W2806811675 modified "2023-10-16" @default.
- W2806811675 title "Novel Method for <scp>l</scp>-Methionine Production Catalyzed by the Aminotransferase ARO8 from <i>Saccharomyces cerevisiae</i>" @default.
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- W2806811675 doi "https://doi.org/10.1021/acs.jafc.8b01451" @default.
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