alexa Characterization of Alkaliphilic, Surfactant Stable and Raw Starch Digesting Α-Amylase from Bacillus subtilis Strain JS-16 | OMICS International
ISSN: 1948-5948

Journal of Microbial & Biochemical Technology
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Research Article

Characterization of Alkaliphilic, Surfactant Stable and Raw Starch Digesting Α-Amylase from Bacillus subtilis Strain JS-16

Gopalakrishnan Menon, Kalpana Mody*, Sumitra Datta and Bhavanath Jha

Discipline of Marine Biotechnology and Ecology, Central Salt and Marine Chemicals Research Institute, Council of Scientific & Industrial Research (CSIR), Gujarat, India

*Corresponding Author:
Dr. Kalpana Mody
Discipline of Marine Biotechnology and Ecology
Central Salt and Marine Chemicals Research Institute
Council of Scientific and Industrial Research (CSIR)
Gijubhai Badheka Marg, Bhavnagar 364 002, Gujarat, India
Tel: +91-278-2561354
Fax: +91-278-2567562
E-mail: [email protected]

Received date: July 25, 2014; Accepted date: August 14, 2014; Published date: August 21, 2014

Citation: Menon G, Mody K, Datta S, Jha B (2014) Characterization of Alkaliphilic, Surfactant Stable and Raw Starch Digesting ?-Amylase from Bacillus subtilis Strain JS-16. J Microb Biochem Technol S8:002. doi: 10.4172/1948-5948.S8-002

Copyright: © 2014 Menon G, 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

An alkali-thermophilic and surfactant stable α-amylase was obtained from Bacillus subtilis strain JS-16, isolated from sludge samples of a soda ash industry, located on west coast of Gujarat. It was active over a wide temperature range (30°C-80°C) exhibiting optimum activity at 50°C and pH 9.0. Unique feature of this amylase was two-fold enhancement of activity in SDS. Three-step purification yielded 15.16-fold purified enzyme with specific activity of 13.5 U/mg proteins. Km and Vmax were 10 mg/ml and 0.2 μmol/min/ml (11.56 μmol/ min/mg protein) respectively. Enzyme activity enhanced with Fe3+ but was strongly inhibited by Hg2+ ions. The amylase hydrolyzed 12% raw wheat starch and 5% corn starch granules after 12 h incubation. Surfactant stability, alkaliphilic nature, activity under wide temperature range and hydrolyses of raw starch makes this amylase a promising candidate for liquid detergent and starch industry.

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