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

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...

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Autores principales: Mohamed, Saleh A., Khan, Jalaluddin A., Al-Bar, Omar A. M., El-Shishtawy, Reda M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270896/
https://www.ncbi.nlm.nih.gov/pubmed/24932573
http://dx.doi.org/10.3390/molecules19068027
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author Mohamed, Saleh A.
Khan, Jalaluddin A.
Al-Bar, Omar A. M.
El-Shishtawy, Reda M.
author_facet Mohamed, Saleh A.
Khan, Jalaluddin A.
Al-Bar, Omar A. M.
El-Shishtawy, Reda M.
author_sort Mohamed, Saleh A.
collection PubMed
description 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.
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spelling pubmed-62708962018-12-21 Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization Mohamed, Saleh A. Khan, Jalaluddin A. Al-Bar, Omar A. M. El-Shishtawy, Reda M. Molecules Article 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. MDPI 2014-06-13 /pmc/articles/PMC6270896/ /pubmed/24932573 http://dx.doi.org/10.3390/molecules19068027 Text en © 2014 by the authors. licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Mohamed, Saleh A.
Khan, Jalaluddin A.
Al-Bar, Omar A. M.
El-Shishtawy, Reda M.
Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization
title Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization
title_full Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization
title_fullStr Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization
title_full_unstemmed Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization
title_short Immobilization of Trichoderma harzianum α-Amylase on Treated Wool: Optimization and Characterization
title_sort immobilization of trichoderma harzianum α-amylase on treated wool: optimization and characterization
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270896/
https://www.ncbi.nlm.nih.gov/pubmed/24932573
http://dx.doi.org/10.3390/molecules19068027
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