BioChem - DOS

Novel Method for L-Methionine Production Catalyzed by the Aminotransferase ARO8 from Saccharomyces cerevisiae

Journal of agricultural and food chemistry

Wu, Yiping; Zha, Musu; Yin, Sheng; Yang, Huaqing; Boutet, Julien; Huet, Robert; Wang, Chengtao; Sun, Baoguo

<P>The aminotransferase ARO8 was proved to play an efficient role in conversion of <SMALL>L</SMALL>-methionine into methionol via the Ehrlich pathway in <I>Saccharomyces cerevisiae</I> in our previous work. In this work, the reversible transamination activity of ARO8 for conversion of &alpha;-keto-&gamma;-(methylthio) butyric acid (KMBA) into <SMALL>L</SMALL>-methionine was confirmed in vitro. ARO8 was cloned from <I>S. cerevisiae</I> S288c and overexpressed in <I>Escherichia coli</I> 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 <SMALL>L</SMALL>-methionine. An approximately 100% conversion rate of KMBA into <SMALL>L</SMALL>-methionine was achieved by optimized enzymatic reaction catalyzed by ARO8. This work fulfilled <SMALL>L</SMALL>-methionine biosynthesis catalyzed by the aminotransferase ARO8 using glutamate and KMBA, which provided a novel method for <SMALL>L</SMALL>-methionine production by enzymatic catalysis with the potential application prospect in industry.</P><BR>[FIG OMISSION]</BR>

2018

American Chemical Society

0021-8561

1520-5118

66

24

pp.6116-6122

10.1021/acs.jafc.8b01451

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART97765731

l-methionine; aminotransferase; ARO8; Saccharomyces cerevisiae