Immobilization of trichoderma harzianum α-Amylase on treated wool: Optimization and characterization

Abstract

α-Amylase from Trichoderma harzianum was covalently immobilized on activated wool by cyanuric chloride. Immobilized á-amylase exhibited 75% of its initial activity after 10 runs. The soluble and immobilized á-amylases exhibited maximum activity at pH values 6.0 and 6.5, respectively. The immobilized enzyme was more thermally stable than the soluble one. Various substrates were hydrolyzed by immobilized á-amylase with high efficiencies compared to those of soluble á-amylase. The inhibition of the immobilized á-amylase by metal ions was low as compared with soluble enzyme. On the basis of the results obtained, immobilized á-amylase could be employed in the saccharification of starch processing. © 2014 by the authors.