Truncation of the unique N-terminal domain improved the thermos-stability and specific activity of alkaline a-amylase Amy703belonging to a new clade from Bacillus pseudofirmus

【Author】

Zhenghui Lu;Qinhong Wang;Sijing Jiang;Guimin Zhang;Yanhe Ma;

【Abstract】

<正>α-Amylases are one of the most important and oldest industrial enzymes,having nearly 30%of the world enzyme market.Alkalineα-amylases having their maximum stability and activity under high pH conditions are of special interest for their potential applications in the textile industries and as ingredients of detergents.But some properties like high alkali-instability and low catalytic efficiency in the commonly used alkaline a-amylases becomes an obstacle for their applications.

【Keywords】

alkaline;amylase;clade;obstacle;instability;melting;maintain;enzymes;created;starch;

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