ISSN: 0973-7510

E-ISSN: 2581-690X

S. Venkatesh1, D. Esther Yazhini2, D. Immanual Gilwax Prabhu1 and S. John Vennison1
1Department of Biotechnology, Bharathidasan Institute of Technology, Anna University, Tiruchirappalli – 620 024. Tamil Nadu, India.
2Department of Civil Engineering, Shri Angalamman College of Engineering & Technology, Tiruchirappalli – 621 105, Tamil Nadu, India.
J Pure Appl Microbiol. 2014;8(3):2513-2518
© The Author(s). 2014
Received: 06/01/2014 | Accepted: 25/03/2014 | Published: 31/06/2014

A gene encoding cellulase enzyme involved in carboxymethylcellulose (CMC) degradation was isolated and sequenced from the ûlamentous fungus, Trichoderma reesei. A DNA fragment of 764bp conferring cellulase activity was cloned in E. coli BL21 and it contained a 726 bp ORF which encoded a protein belonging to glycosyl hydrolase family 45 and was classified as endoglucanase. It showed a maximum cellulase activity of 11.75 IU/g, at pH 5.5 and at 37oC. The SDS–PAGE and zymogram analyses showed a protein band with a molecular weight of about 24,420 Da confirming endoglucanase expression.


Cellulase, Endoglucanase gene, cDNA, E.coli BL21 and Trichoderma reesei

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