Potential thermostable mutants of endoglucanase I from fusarium oxysporum

Lignocellulose is the most abundant biopolymer on earth and it is a good renewable energy source. Thermostable enzymes have several benefits in various industrial applications. Among the benefits are they allow the use of increased substrate concentration in the reaction mixture, as the viscosity wi...

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Main Authors:	Ibrahim Ali , Noorbatcha, Hamzah, Mohd. Salleh
Format:	Conference or Workshop Item
Language:	English English English
Published:	2015
Subjects:	TP248.13 Biotechnology
Online Access:	http://irep.iium.edu.my/46338/ http://irep.iium.edu.my/46338/1/ICAST_2015_Enrichment_abstract_ENV-EO9.pdf http://irep.iium.edu.my/46338/2/icast_brochure2015.pdf http://irep.iium.edu.my/46338/3/Icast_2015_Thermostable_EG_I.pdf

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recordtype	eprints
spelling	iium-463382016-01-06T07:39:03Z http://irep.iium.edu.my/46338/ Potential thermostable mutants of endoglucanase I from fusarium oxysporum Ibrahim Ali , Noorbatcha Hamzah, Mohd. Salleh TP248.13 Biotechnology Lignocellulose is the most abundant biopolymer on earth and it is a good renewable energy source. Thermostable enzymes have several benefits in various industrial applications. Among the benefits are they allow the use of increased substrate concentration in the reaction mixture, as the viscosity will drop at higher temperature which eventually will improve product yield and reduces capital and processing costs. This research intends to predict computationally, and develop experimentally, a thermostable mutant endoglucanase that can operate at higher temperature as required by industrial processes. Our preliminary computational data based on rational design approach suggest that quintuple mutant, T224E/G229A/S230F/S231E/N321R, of an endoglucanase from a pathogenic fungus, Fusarium oxysporum, can potentially remain active at higher temperature (80oC) compared to its current operating temperature (<60oC). In our effort to experimentally produce this quintuple mutant we have successfully produced a single mutant, T224E, and a triple mutant, G229A/S230F/S231E, via site directed mutagenesis. We are reporting here the characterization results of these two mutants as compared to the wild type. Keywords: Thermostable enzymes, mutant endoglucanases, Fusarium oxysporum 2015 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/46338/1/ICAST_2015_Enrichment_abstract_ENV-EO9.pdf application/pdf en http://irep.iium.edu.my/46338/2/icast_brochure2015.pdf application/pdf en http://irep.iium.edu.my/46338/3/Icast_2015_Thermostable_EG_I.pdf Ibrahim Ali , Noorbatcha and Hamzah, Mohd. Salleh (2015) Potential thermostable mutants of endoglucanase I from fusarium oxysporum. In: 5th International Conference on the Advancement in Science and Technology (ICAST 2015), 10-12 AUGUST 2015 , Impiana Resort Cherating, Pahang MALAYSIA. (Unpublished)
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English English English
topic	TP248.13 Biotechnology
spellingShingle	TP248.13 Biotechnology Ibrahim Ali , Noorbatcha Hamzah, Mohd. Salleh Potential thermostable mutants of endoglucanase I from fusarium oxysporum
description	Lignocellulose is the most abundant biopolymer on earth and it is a good renewable energy source. Thermostable enzymes have several benefits in various industrial applications. Among the benefits are they allow the use of increased substrate concentration in the reaction mixture, as the viscosity will drop at higher temperature which eventually will improve product yield and reduces capital and processing costs. This research intends to predict computationally, and develop experimentally, a thermostable mutant endoglucanase that can operate at higher temperature as required by industrial processes. Our preliminary computational data based on rational design approach suggest that quintuple mutant, T224E/G229A/S230F/S231E/N321R, of an endoglucanase from a pathogenic fungus, Fusarium oxysporum, can potentially remain active at higher temperature (80oC) compared to its current operating temperature (<60oC). In our effort to experimentally produce this quintuple mutant we have successfully produced a single mutant, T224E, and a triple mutant, G229A/S230F/S231E, via site directed mutagenesis. We are reporting here the characterization results of these two mutants as compared to the wild type. Keywords: Thermostable enzymes, mutant endoglucanases, Fusarium oxysporum
format	Conference or Workshop Item
author	Ibrahim Ali , Noorbatcha Hamzah, Mohd. Salleh
author_facet	Ibrahim Ali , Noorbatcha Hamzah, Mohd. Salleh
author_sort	Ibrahim Ali , Noorbatcha
title	Potential thermostable mutants of endoglucanase I from fusarium oxysporum
title_short	Potential thermostable mutants of endoglucanase I from fusarium oxysporum
title_full	Potential thermostable mutants of endoglucanase I from fusarium oxysporum
title_fullStr	Potential thermostable mutants of endoglucanase I from fusarium oxysporum
title_full_unstemmed	Potential thermostable mutants of endoglucanase I from fusarium oxysporum
title_sort	potential thermostable mutants of endoglucanase i from fusarium oxysporum
publishDate	2015
url	http://irep.iium.edu.my/46338/ http://irep.iium.edu.my/46338/1/ICAST_2015_Enrichment_abstract_ENV-EO9.pdf http://irep.iium.edu.my/46338/2/icast_brochure2015.pdf http://irep.iium.edu.my/46338/3/Icast_2015_Thermostable_EG_I.pdf
first_indexed	2023-09-18T21:05:58Z
last_indexed	2023-09-18T21:05:58Z
_version_	1777410935338565632

Potential thermostable mutants of endoglucanase I from fusarium oxysporum

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