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Expression of a Fusarium oxysporum endoglucanase in kluyveromyces lactis

Moukit, Farid and Amid, Azura and Mohd. Salleh, Hamzah (2011) Expression of a Fusarium oxysporum endoglucanase in kluyveromyces lactis. In: 2nd International Conference on Biotechnology Engineering (ICBioE 2011), 17-19 May 2011, The Legend Hotel, Kuala Lumpur.

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Abstract

Cellulose is the main component in plant cell wall and thus the most abundant biopolymer on earth. Endoglucanase is one of the key constituent of a complex multi-enzyme system collectively known as cellulase which degrades cellulose into glucose. Cellulase has been used in various industries such as textile, detergent, food and feed, pulp and paper, and recently in bio-fuel industries. This research intends to clone and characterize functional endoglucanase enzyme from a thermophilic pathogenic plant fungus, Fusarium oxysporum, in suitable eukaryotic expression system (Kluyveromyces lactis). Kluyveromyces lactis have many advantages of higher eukaryotic expression systems such as: protein processing, protein folding, and post-translational modification. While being as easy to manipulate as ‘E. coli’, they give higher expression levels. This research will also optimize the process conditions required for the maximal formation of functional recombinant endoglucanase, followed by purification of the recombinant enzyme before determining the characteristics of the recombinant endoglucanase such as stability (pH, temperature) and activity (substrates, effectors and inhibitors).

Item Type: Conference or Workshop Item (Full Paper)
Additional Information: 3688/16202
Uncontrolled Keywords: component; Endoglucanase, Kluyveromyces lactis, Fusarium oxysporum, optimization.
Subjects: T Technology > TP Chemical technology > TP248.13 Biotechnology
Kulliyyahs/Centres/Divisions/Institutes: Kulliyyah of Engineering > Department of Biotechnology Engineering
Depositing User: Dr Azura Amid
Date Deposited: 02 Feb 2012 12:26
Last Modified: 02 Feb 2012 15:18
URI: http://irep.iium.edu.my/id/eprint/16202

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