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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Improving the Catalytic Performance of a Talaromyces leycettanus alpha-Amylase by Changing the Linker Length
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Improving the Catalytic Performance of a Talaromyces leycettanus alpha-Amylase by Changing the Linker Length

机译：Improving the Catalytic Performance of a Talaromyces leycettanus alpha-Amylase by Changing the Linker Length

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摘要

A novel alpha-amylase, Amyl3A, that consists of these domains was identified in Talaromyces leycettanus JCM12802: catalytic TIM-barrel fold, domain B, domain C, Thr/Ser-rich linker region, and C-terminal CBM20 domain. The wild type and three mutant, enzymes were then expressed in Pichia pastoris GS115 to identify the roles of linker length (Amy13A21 and Amy13A33) and CBM20 (Amyl3A-CBM) in catalysis. All enzymes had similar enzymatic properties, exhibiting optimal activities at pH 4.5-5.0 and 55-60 C, but varied in catalytic performance. When using soluble starch as the substrate, Amy13A21 and Amy13A33 showed specific activities (926.3 and 537.8 units/mg, respectively, vs 252.1 units/mg) and catalytic efficiencies (k(cat)/k(m), 25.7 and 22.0 mL s(-1) mg(-1), respectively, vs 15.4 mL s(-1) mg(-1)) higher than those of the wild type, while Amy13A-CBM performed worse during catalysis. This study reveals the key roles of the CBM and linker length in the catalysis of GH13 alpha-amylase.

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