Producing mutant alfa-galactosidase with increased thermal stability
By analyzing the three-dimensional structure of alpha-galactosidase from marine bacterium Pseudoalteromonas sp. KMM 701, the point mutations of amino acid residues of the enzyme for obtaining more thermostable enzyme modifications were predicted by PCR-mediated site-directed mutagenesis. The mutant alpha-galactosidase with amino acid substitution C493N in the active center has thermal stability increased by 15 % as compared with the wild type of enzyme.