Detection of thermal stability of protein site mutation based on genetic algorithm

Abstract

In order to improve the thermal stability of protein site-specific mutation, a method based on genetic algorithm was proposed to detect the thermal stability of protein site-specific mutation using Escherichia coli phytase APPA as experimental material. Based on the principle of genetic algorithm for predicting protein structures, the author designed ten mutation sites on the acid enzyme APPA to obtain APPAM10, tested the optimal pH and temperature of the two and analyzed the effect of multiple mutation sites on the temperature stability of the phytase APPA. The relative activity of APPA was greatly affected by temperature, while the residual relative activity of APPA was higher in the mutant, and K24E was the mutant with better comprehensive properties. The optimal pH value of APPA and APPAM10 was about 4, but the optimal temperature of APPAM10 was slightly higher than that of APPA. With the increase in temperature, the residual activity and dissolution of APPAM10 were higher. The temperature was higher than that of APPA. This method can effectively detect the thermal stability of protein site mutation, and the pH stability and thermal stability of APPA protein after site mutation are better than those before mutation.