High Production of Maltooligosaccharides in the Starch Liquefaction Process: A Study on the Hyperthermophilic Mechanism of ?-Amylase

文献类型： 外文期刊

第一作者： Liao, Min

作者： Liao, Min;Dong, Ruyue;Li, Lanxue;Wang, Yaru;Bai, Yingguo;Luo, Huiying;Yao, Bin;Huang, Huoqing;Tu, Tao;Liu, Xiaoqing

作者机构：

关键词： ?-amylase; hyperthermophilic mechanism; site-directed mutagenesis; starch liquefaction; maltooligosaccharide

期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.1； 五年影响因子：6.3 ）

ISSN： 0021-8561

年卷期： 2023 年 71 卷 16 期

页码：

收录情况： SCI

摘要： The efficient production of high-value-added bioproducts from starchy substances requires alpha-amylases with hyperthermophilic properties for industrial starch liquefaction. In this study, two hyperthermophilic alpha-amylases with significant differences in thermostability, PfAmy and TeAmy, were comparatively studied through structural analysis, domain swapping, and site-directed mutagenesis, finding that three residues, His152, Cys166, and His168, located in domain B were the main contributors to hyperthermostability. The effects of these three residues were strongly synergistic, causing the optimum temperature for the mutant K152H/A166C/E168H of TeAmy to shift to 95-100 degrees C and stabilize at 90 degrees C without Ca2+. Compared to PfAmy and TeAmy, the mutant K152H/A166C/E168H, respectively, exhibited 1.7-and 2.5-times higher starch hydrolysis activity at 105 degrees C and pH 5.5 (10411 +/- 70 U/mg) and released 1.1-and 1.7-times more maltooligosaccharides from 1% starch. This work has interpreted the hyperthermophilic mechanism of alpha-amylase and thereby providing a potential candidate for the efficient industrial conversion of starch to bioproducts.

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