热稳定性
蛋白质工程
合理设计
定向进化
蛋白质设计
蛋白质折叠
生化工程
合成生物学
生物制药
计算机科学
工程设计过程
酶
热稳定性
计算生物学
突变体
生物化学
化学
蛋白质结构
材料科学
工程类
生物
纳米技术
遗传学
有机化学
基因
机械工程
作者
Vinutsada Pongsupasa,Piyanuch Anuwan,Somchart Maenpuen,Thanyaporn Wongnate
出处
期刊:Methods in molecular biology
日期:2021-11-24
卷期号:: 159-178
被引量:12
标识
DOI:10.1007/978-1-0716-1826-4_9
摘要
The fundamentals of thermostability engineering need to be carried out for proteins with low thermal stability to expand their utilization. Thus, comprehension of the thermal stability regulating factors of proteins is needful for the engineering of their thermostability. Protein engineering aims to overcome their natural limitations in tough conditions by refining protein stability and activity. Rational-design approach requires a crystal structure dataset along with the biophysical information, protein function, and sequence-based data, especially consensus sequence that is favorable for the protein folding during natural evolution. It can be attained by either single- or multiple-point mutation, by which amino acids are changed. In fact, these mutation approaches show several benefits. For example, the offered mutations are produced after an evaluation and design, which raise the chance to acquire favorable mutations. The rational-design engineering can improve the biochemical properties of enzymes, including the kinetic behaviors, substrate specificity, thermostability, and organic solvent tolerance. Moreover, this approach considerably reduces the library size, so less effort and time can be employed. Here, we apply the computational algorithms and programs with experiments to create thermostable enzymes that will be beneficial for future applications.
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