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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/46338/1/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
http://irep.iium.edu.my/46338/
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spelling my.iium.irep.463382021-07-01T00:34:02Z 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)
institution Universiti Islam Antarabangsa Malaysia
building IIUM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider International Islamic University Malaysia
content_source IIUM Repository (IREP)
url_provider http://irep.iium.edu.my/
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/46338/1/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
http://irep.iium.edu.my/46338/
_version_ 1705056476794454016
score 13.211869

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