A High Salt Stable ÃÂ-Amylase by Bacillus Sp. MRS6 Isolated from Municipal Solid Waste; Purification, Characterization and Solid State FermentationSmarajit Maiti1,2*, Sudipta Roy1 and Sumit Sahoo1
2Department of Biochemistry and Biotechnology, Cell and Molecular Therapeutics Laboratory, Oriental Institute of Science and Technology (OIST), Vidyasagar University, Midnapore-721102, West Bengal, India
- *Corresponding Author:
- Smarajit Maiti
Associate Professor and Head
Post Graduate Department of Biochemistry and Biotechnology
Cell and Molecular Therapeutics Laboratory
OIST, Vidyasagar University
Midnapore -721101, India
E-mail: [email protected]
Received date: July 25, 2016; Accepted date: September 09, 2016; Published date: September 14, 2016
Citation: Maiti S, Roy S, Sahoo S (2016) A High Salt Stable ɑ-Amylase by Bacillus Sp. MRS6 Isolated from Municipal Solid Waste; Purification, Characterization and Solid State Fermentation. Enz Eng 5: 150. doi:10.4172/2329-6674.1000150
Copyright: © 2015 Maiti S, 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.
Salt-tolerant alkaline amylase producing Bacillus sp. MRS6 was isolated from three municipal waste disposal site of Medinipur town in the Paschim Medinipur district of southern West Bengal, India. The strain had been characterized from a polyphasic approach. Extracellular enzyme production was carried out in mineral salt media at pH-7, 35°C with 2% soluble starch as sole carbon source. It was found that the amylase, produced by the salttolerant strain possessed high activity in a range of alkaline pH (6-9), with pH-8 as optimum. An incubation period of 30 min at 35°C was found as optimum temperature condition of its activity. This alkaliphilic, salt-tolerant enzyme was found to stay stable upto 80°C, 4M NaCl. Mn2+, Ca2+ plays critical role in >80% increasing of this enzyme activity. EDTA, β-merkeptoethanol and detergents strongly inhibit enzyme activity. This enzyme was able to ferment the solid substrates i.e. wheat bran greater than rice husk. This enzyme was purified partially by cold acetone precipitation and the molecular mass was found to be 55 kDa by SDS PAGE. The present findings suggested the enzyme to be halophilic alkaline amylase. The present enzyme is of great significance in present day biotechnology with applications ranging from food, fermentation, textile, detergent to paper industries.