Unknown

Dataset Information

0

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


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, Ni(2+) (32%), K(+) (44%), and Cu(2+) (56%) increased the enzyme activity while EDTA (7%), SDS (7%), Hg(2+) (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.

SUBMITTER: Kuzu SB 

PROVIDER: S-EPMC3532916 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Kuzu Secil Berna SB   Güvenmez Hatice Korkmaz HK   Denizci Aziz Akin AA  

Biotechnology research international 20121213


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  ...[more]

Similar Datasets

| S-EPMC3622971 | biostudies-literature
| S-EPMC3208992 | biostudies-literature
| S-EPMC5289684 | biostudies-literature
| S-EPMC182717 | biostudies-literature
| S-EPMC167511 | biostudies-other
| S-EPMC8033632 | biostudies-literature
| S-EPMC6508605 | biostudies-literature
| S-EPMC8028025 | biostudies-literature
| S-EPMC7586909 | biostudies-literature
| S-EPMC7586917 | biostudies-literature