利用随机突变探讨影响α—淀粉酶催化活性的氨基酸位点

α-Amylase is widely used in biotechnology industries such as food,textile and detergent.It occupies an important position in the domestic and international enzyme market.An important reason that amylase can achieve its function is it has catalysis domain,which is a very basilic domain,and the function of the catalysis domain mainly depends on catalytic active site.So changing the base of the active site or the base around the active site may affect a lot on α-amylase.This article mainly describes using random mutagenesis of the α-amylase by error-prone PCR,detecting the amylase activity of the mutant strains,and then sequencing the mutants.8 available mutants was picked to do further analysis and prediction of 3D structure.Choosing the mutant with the highest enzyme activity improvement as a further research target molecule,the potential structure changes were predicted by replacement of amino acid residue at the mutant site with other 18 residues.