Table of Contents
Biotechnology Research International
Volume 2012, Article ID 135498, 6 pages
http://dx.doi.org/10.1155/2012/135498
Research Article

Production of a Thermostable and Alkaline Chitinase by Bacillus thuringiensis subsp. kurstaki Strain HBK-51

1Biotechnology & Molecular Biology Division, Department of Biology, Cukurova University, 01330 Adana, Turkey
2Research Institute for Genetic Engineering and Biotechnology, The Scientific and Technical Research Council of Turkey (TUBITAK), Marmara Research Center Campus, Gebze-Kocaeli 41470, Turkey

Received 21 September 2012; Accepted 14 November 2012

Academic Editor: Triantafyllos Roukas

Copyright © 2012 Secil Berna Kuzu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

This paper reports the isolation and identification of chitinase-producing Bacillus from chitin-containing wastes, production of a thermostable and alkaline chitinasese, and enzyme characterization. Bacillus thuringiensis subsp. kurstaki HBK-51 was isolated from soil and was identified. Chitinase was obtained from supernatant of B. thuringiensis HBK-51 strain and showed its optimum activity at 110°C and at pH 9.0. Following 3 hours of incubation period, the enzyme showed a high level of activity at 110°C (96% remaining activity) and between pH 9.0 and 12.0 (98% remaining activity). Considering these characteristics, the enzyme was described as hyperthermophile-thermostable and highly alkaline. Two bands of the enzyme weighing 50 and 125 kDa were obtained following 12% SDS-PAGE analyses. Among the metal ions and chemicals used, Ni2+ (32%), K+ (44%), and Cu2+ (56%) increased the enzyme activity while EDTA (7%), SDS (7%), Hg2+ (11%), and ethyl-acetimidate (20%) decreased the activity of the enzyme. Bacillus thuringiensis subsp. kurstaki HBK-51 is an important strain which can be used in several biotechnological applications as a chitinase producer.