alexa Synthesizing a Cellulase like Chimeric Protein by Recombinant Molecular Biology Techniques
ISSN: 2155-9821

Journal of Bioprocessing & Biotechniques
Open Access

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Short Communication

Synthesizing a Cellulase like Chimeric Protein by Recombinant Molecular Biology Techniques

Hirendra Nath Banerjee*, Christopher Krauss, Valerie Smith, Kelly Mahaffey and Ava Boston

Department of Natural Pharmacy and Health Sciences, Elizabeth City State University, University of North Carolina, Elizabeth City, NC-27909, USA

*Corresponding Author:
Hirendra Nath Banerjee
Professor, Department of Natural Pharmacy and Health Sciences
Elizabeth City State University
University of North Carolina, Elizabeth City
NC-27909, USA
Tel: 2523353241
Fax: 2523353697
E-mail: [email protected]

Received date: March 18, 2016; Accepted date: June 25, 2016; Published date: June 30, 2016

Citation: Banerjee HN, Krauss C, Smith V, Mahaffey K, Boston A (2016) Synthesizing a Cellulase like Chimeric Protein by Recombinant Molecular Biology Techniques. J Bioprocess Biotech 6: 285. doi:10.4172/2155-9821.1000285

Copyright: © 2016 Banerjee HN, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

In order to meet the Renewable Fuels Standard demands for 30 billion gallons of biofuels by the end of 2020, new technologies for generation of cellulosic ethanol must be exploited. Breaking down cellulose by cellulase enzyme is very important for this purpose but this is not thermostable and degrades at higher temperatures in bioreactors. Towards creation of a more ecologically friendly method of rendering bioethanol from cellulosic waste, we attempted to produce recombinant higher temperature resistant cellulases for use in bioreactors. The project involved molecular cloning of genes for cellulose-degrading enzymes based on bacterial source, expressing the recombinant proteins in E. coli and optimizing enzymatic activity. We were able to generate in vitro bacterial expression systems to produce recombinant His-tag purified protein which showed cellulase like activity.

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