Liu Lixing, Cai Lixi, Chu Yunmeng, Zhang Min
College of Basic Medicine, Putian University, Putian, 351100, Fujian, China.
Putian University Key Laboratory of Translational Tumor Medicine in Fujian Province, Putian, 351100, Fujian, China.
AMB Express. 2022 May 6;12(1):50. doi: 10.1186/s13568-022-01394-x.
Agarase is a natural catalyst with a good prospect in the industry. However, most of the currently discovered β-agarases are unsuitable for relatively high-temperature and high-pressure conditions required by industrial production. In this study, molecular dynamics simulations were first used to investigate the dynamic changes of folding and unfolding of mesophile and thermophile β-agarases (i.e., 1URX and 3WZ1) to explore the thermostability mechanism at three high temperatures (300 K, 400 K, and 500 K). Results showed that the sequence identity of 3WZ1 and 1URX reaches 48.8%. 1URX has a higher thermal sensitivity and less thermostability than 3WZ1 as more thermostable regions and hydrogen bonds exist in 3WZ1 compared with 1URX. The structures of 1URX and 3WZ1 become unstable with increasing temperatures up to 500 K. The strategies to increase the thermostability of 1URX and 3WZ1 are discussed. This study could provide insights into the design and modification of β-agarases at a high temperature.
琼脂酶是一种在工业领域具有良好前景的天然催化剂。然而，目前发现的大多数β-琼脂酶并不适用于工业生产所需的相对高温和高压条件。在本研究中，首先使用分子动力学模拟来研究嗜温菌和嗜热菌β-琼脂酶（即1URX和3WZ1）折叠和展开的动态变化，以探索在三个高温（300 K、400 K和500 K）下的热稳定性机制。结果表明，3WZ1和1URX的序列同一性达到48.8%。与1URX相比，3WZ1具有更多的热稳定区域和氢键，因此1URX比3WZ1具有更高的热敏感性和更低的热稳定性。随着温度升高至500 K，1URX和3WZ1的结构变得不稳定。讨论了提高1URX和3WZ1热稳定性的策略。本研究可为高温下β-琼脂酶的设计和修饰提供见解。
