Next Article in Journal
Reduction of the Nitro Group to Amine by Hydroiodic Acid to Synthesize o-Aminophenol Derivatives as Putative Degradative Markers of Neuromelanin
Next Article in Special Issue
Catalytic Behavior of Lipase Immobilized onto Congo Red and PEG-Decorated Particles
Previous Article in Journal
Tetrabutylammonium Bromide (TBABr)-Based Deep Eutectic Solvents (DESs) and Their Physical Properties
Previous Article in Special Issue
Evaluation of Styrene-Divinylbenzene Beads as a Support to Immobilize Lipases
Molecules 2014, 19(6), 8027-8038; doi:10.3390/molecules19068027
Article

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

1,2,* , 1
,
1
 and
3,4
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)
View Full-Text   |   Download PDF [541 KB, uploaded 18 June 2014]   |  

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.
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 (CC BY 3.0).
SciFeed

Share & Cite This Article

Further Mendeley | CiteULike
Export to BibTeX |
EndNote |
RIS
MDPI and ACS Style

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.

View more citation formats

Related Articles

Article Metrics

For more information on the journal, click here

Comments

[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert