Abstract
Acid stability of Bacillus licheniformis alpha amylase (BLA) was improved by error-prone polymerase chain reaction. The mutated BLA gene was expressed in Escherichia coli. An acid stability double mutant (K344R/H405R in BLA) was isolated. Two single mutants K344R and H405R were obtained by the way of site-directed mutagenesis. The enzymes (BLA) of the three mutants were isolated and characterized. Kinetic studies showed that the kcat/Km values of the mutants K344R, H405R, and K344R/H405R under pH 4.5 were about 8-, 11.5-, and 17.7-times higher than that of the wild type enzyme. As revealed by the structure models of the wild-type and mutant enzymes, the amino acids substituted of R344 and R405 in the BLA contribute to its acid stability.
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