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Molecules 2014, 19(6), 8027-8038; doi:10.3390/molecules19068027

Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization

1,2,* , 1
Received: 8 March 2014 / Revised: 4 June 2014 / Accepted: 6 June 2014 / Published: 13 June 2014
(This article belongs to the Special Issue Enzyme Immobilization)
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α-Amylase from Trichoderma harzianum was covalently immobilized on activated wool by cyanuric chloride. Immobilized α-amylase exhibited 75% of its initial activity after 10 runs. The soluble and immobilized α-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 α-amylase with high efficiencies compared to those of soluble α-amylase. The inhibition of the immobilized α-amylase by metal ions was low as compared with soluble enzyme. On the basis of the results obtained, immobilized α-amylase could be employed in the saccharification of starch processing.
Keywords: Trichoderma harzianum; α-amylase; immobilized enzyme; optimization Trichoderma harzianum; α-amylase; immobilized enzyme; optimization
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Mohamed, S.A.; Khan, J.A.; Al-Bar, O.A.M.; El-Shishtawy, R.M. Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization. Molecules 2014, 19, 8027-8038.

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