Abstract
Bacillus licheniformis 44MB82-A α-amylase was purified and immobilized on five silica supports. The relative activity of the immobilized amylase represented from 22 to 40% of the activity of the bound protein. The immobilized enzyme was used for repeated batch hydrolysis of soluble starch. Arylamine CPG and Spherosyl XOA 200 were found to be suitable as carriers and the enzyme immobilized on them retained 60% of its initial activity after reuse. Considerable changes in the hydrolysis products and the inability of the immobilized α-amylase to hydrolyse some malto-oligosaccharides were observed.
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