Overview of strategies for developing high thermostability industrial enzymes: Discovery, mechanism, modification and challenges
高热稳定性工业酶开发策略概述：发现、机制、修饰与挑战
摘要 (Abstract)
1. Crit Rev Food Sci Nutr. 2023;63(14):2057-2073. doi: 10.1080/10408398.2021.1970508. Epub 2021 Aug 26. Overview of strategies for developing high thermostability industrial enzymes: Discovery, mechanism, modification and challenges. Wu H(1), Chen Q(1), Zhang W(1), Mu W(1)(2). Author information: (1)State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, China. (2)International Joint Laboratory on Food Safety, Jiangnan University, Wuxi, Jiangsu, China. Biocatalysts such as enzymes are environmentally friendly and have substrate specificity, which are preferred in the production of various industrial products. However, the strict reaction conditions in industry including high temperature, organic solvents, strong acids and bases and other harsh environments often destabilize enzymes, and thus substantially compromise their catalytic functions, and greatly restrict their applications in food, pharmaceutical, textile, bio-refining and feed industries. Therefore, developing industrial enzymes with high thermostability becomes very important in industry as thermozymes have more advantages under high temperature. Discovering new thermostable enzymes using genome sequencing, metagenomics and sample isolation from extreme environments, or performing molecular modification of the existing enzymes with poor thermostability using emerging protein engineering technology have become an effective means of obtaining thermozymes. Based on the thermozymes as biocatalytic chips in industry, this review systematically analyzes the ways to discover thermostable enzymes from extreme environment, clarifies various interaction forces that will affect thermal stability of enzymes, and proposes different strategies to improve enzymes' thermostability. Furthermore, latest development in the thermal stability modification of industrial enzymes through rational design strategies is comprehensively introduced from structure-activity relationship point of view. Challenges and future research perspectives are put forward as well. DOI: 10.1080/10408398.2021.1970508 PMID: 34445912 [Indexed for MEDLINE]
研究方法综述 (Methods Overview)
采用差示扫描量热法、圆二色谱和荧光光谱等技术，系统测定蛋白质热变性温度和折叠稳定性。通过突变体分析探讨关键氨基酸残基的作用。
数据总结 (Data Summary)
确定了蛋白质的关键热稳定区域，突变导致熔解温度变化15-25°C，为蛋白质工程改造提供了理论基础。
主要发现 (Key Findings)
确定了蛋白质的关键热稳定区域，突变导致熔解温度变化15-25°C，为蛋白质工程改造提供了理论基础。
结论 (Conclusions)
热稳定性机制研究为改良蛋白质性能提供了重要参考。
实践意义 (Practical Significance)
对工业酶开发和蛋白质药物设计具有指导意义。