Alpha amylase (EC3.2.1.1), one of more widespread enzymes in the industrial world, is a glycoside hydrolase. It hydrolyzes the α- (1,4) glucoside linkage between the glucose units of a polysaccharide. Microbial amylases, particularly those from Bacillus genus are more in demand than those from other sources. Alpha-amylases have potential application in wide number of industrial applications such as textile, paper, detergent, food, fermentation and pharmaceutical industries. Recombinant DNA technology for amylase production involves the selection of an efficient amylase gene, its insertion into an appropriate vector system, transformation in an efficient bacterial system to produce high amount of recombinant protein. In this context, the aim of this work is the overexpression of anαamylase gene from Bacillus subtilisUS572in E. coli strain and the characterization of the recombinant amylase which is an interesting candidate for biotechnological applications.
Biochemical and molecular characterization of a recombinant α-amylase from Bacillus subtilis
Perduca Massimiliano;
2018-01-01
Abstract
Alpha amylase (EC3.2.1.1), one of more widespread enzymes in the industrial world, is a glycoside hydrolase. It hydrolyzes the α- (1,4) glucoside linkage between the glucose units of a polysaccharide. Microbial amylases, particularly those from Bacillus genus are more in demand than those from other sources. Alpha-amylases have potential application in wide number of industrial applications such as textile, paper, detergent, food, fermentation and pharmaceutical industries. Recombinant DNA technology for amylase production involves the selection of an efficient amylase gene, its insertion into an appropriate vector system, transformation in an efficient bacterial system to produce high amount of recombinant protein. In this context, the aim of this work is the overexpression of anαamylase gene from Bacillus subtilisUS572in E. coli strain and the characterization of the recombinant amylase which is an interesting candidate for biotechnological applications.File | Dimensione | Formato | |
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