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Shin, Sun-Mi,Kim, Hana,Joo, Yunhye,Lee, Sang-Jae,Lee, Yong-Jik,Lee, Sang Jun,Lee, Dong-Woo American Chemical Society 2014 Journal of agricultural and food chemistry Vol.62 No.50
<P>The <I>gadB</I> gene encoding glutamate decarboxylase (GAD) from <I>Lactobacillus plantarum</I> was cloned and expressed in <I>Escherichia coli</I>. The recombinant enzyme exhibited maximal activity at 40 °C and pH 5.0. The 3D model structure of <I>L. plantarum</I> GAD proposed that its C-terminal region (Ile454–Thr468) may play an important role in the pH dependence of catalysis. Accordingly, C-terminally truncated (Δ3 and Δ11 residues) mutants were generated and their enzyme activities compared with that of the wild-type enzyme at different pH values. Unlike the wild-type GAD, the mutants showed pronounced catalytic activity in a broad pH range of 4.0–8.0, suggesting that the C-terminal region is involved in the pH dependence of GAD activity. Therefore, this study may provide effective target regions for engineering pH dependence of GAD activity, thereby meeting industrial demands for the production of γ-aminobutyrate in a broad range of pH values.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jafcau/2014/jafcau.2014.62.issue-50/jf504656h/production/images/medium/jf-2014-04656h_0007.gif'></P>