Ban Xiaofeng, Xie Xiaofang, Li Caiming, Gu Zhengbiao, Hong Yan, Cheng Li, Kaustubh Bhalerao, Li Zhaofeng
School of Food Science and Technology, Jiangnan University, Wuxi 214122, People's Republic of China.
State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi 214122, People's Republic of China; School of Food Science and Technology, Jiangnan University, Wuxi 214122, People's Republic of China; Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, Wuxi, Jiangsu 214122, People's Republic of China.
Food Chem. 2021 Aug 30;354:129475. doi: 10.1016/j.foodchem.2021.129475. Epub 2021 Mar 8.
The α-amylases are the most widely used industrial enzymes, and are particularly useful as liquifying enzymes in industrial processes based upon starch. Since starch liquefication is carried out at evaluated temperatures, typically above 60 °C, there is substantial demand for thermostable α -amylases. Most naturally occurring α -amylases exhibit moderate thermostability, so substantial effort has been invested in attempts to increase their thermostability. One structural feature that has the potential to increase protein thermostability is the introduction of salt bridges. However, not every salt bridge contributes to protein thermostability. The salt bridges in amylases have their characteristics in terms of distribution, configuration and location. The summary of these features helps to introduce new salt bridges based on the characteristics. This review focuses on salt bridges of α-amylases, both naturally present and introduced using mutagenesis. Its aim is to provide a bird's eye view of distribution, configuration, location of desirable salt bridges.
α-淀粉酶是应用最为广泛的工业酶，尤其作为基于淀粉的工业生产过程中的液化酶非常有用。由于淀粉液化是在较高温度下进行的，通常高于60°C，因此对耐热α-淀粉酶有大量需求。大多数天然存在的α-淀粉酶表现出中等的热稳定性，所以人们投入了大量精力来提高它们的热稳定性。一个有可能提高蛋白质热稳定性的结构特征是引入盐桥。然而，并非每个盐桥都有助于蛋白质的热稳定性。淀粉酶中的盐桥在分布、构型和位置方面都有其特点。对这些特征的总结有助于根据其特点引入新的盐桥。本综述聚焦于α-淀粉酶中的盐桥，包括天然存在的以及通过诱变引入的。其目的是对理想盐桥的分布、构型和位置进行全景式的介绍。
