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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
Biochemistry Department, Faculty of Science, King Abdulaziz University, 21589, Jeddah, Kingdom of Saudi Arabia
2
Molecular Biology Department, National Research Center, Dokki, 12622, Cairo, Egypt
3
Chemistry Department, Faculty of Science, King Abdulaziz University, 21589, Jeddah, Kingdom of Saudi Arabia
4
Dyeing, Printing and Textile Auxiliaries Department, Textile Research Division, National Research Center, Dokki, 12622, Cairo, Egypt
*
Author to whom correspondence should be addressed.
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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Abstract

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. View Full-Text
Keywords: Trichoderma harzianum; α-amylase; immobilized enzyme; optimization Trichoderma harzianum; α-amylase; immobilized enzyme; optimization
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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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