ISSN: 2155-6199

Journal of Bioremediation & Biodegradation
Open Access

Our Group organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations
700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)
  • Research Article   
  • J Bioremediat Biodegrad 8:417,
  • DOI: 10.4172/2155-6199.1000417

Purification and Characterization of �?±-Amylase from Bacillus subtilis Isolated from Cassava Processing Sites

Alabi Gbenga1, Sanni David1, Bamidele Femi1 and Adeleke Bartholomew Saanu2*
1Department of Biochemistry, Federal University of Technology, Akure, Nigeria
2Department of Microbiology, Federal University of Technology, Akure, Nigeria
*Corresponding Author : Adeleke Bartholomew Saanu, Department of Microbiology, Federal University of Technology, Akure, Nigeria, Tel: +2347065058110, Email: microbade@yahoo.com

Received Date: Sep 29, 2017 / Accepted Date: Oct 26, 2017 / Published Date: Oct 30, 2017

Abstract

This study was designed to purify and characterize of α-amylase from pure strain of Bacillus subtilis. The crude α- amylase was purified by ammonium sulphate precipitation, then loaded on DEAE Sephadex A-50 ion exchange chromatography and gel filtration. The effect of pH, temperature and metal ions were investigated on the purified enzyme. The single protein band on SDS-PAGE suggested that the enzyme was homogenous. Two different activity peaks were observed in ion exchange chromatography designated pool A and pool B with the 8% and 4% yield, 15.93 and 6.44 purification fold and specific activity 2.55 μmol/min/mg and 1.03 μmol/min/mg respectively. The two fractions revealed the same optimum pH 7.0 for the α-amylase activity while the enzyme was relatively stable at pH 4.0 and 7.0 between 20 to 40 minutes and 60 to 80 minutes for pool A and pH 8.0 between 40 and 100 minutes for pool B. At 40°C, optimum temperature was reached, and amylase activity was maintained at 75% and 70% temperature stability between 60 to 80 minutes for pool A and B, less than 20%, the residual activity at 60°C and 70°C was recorded. The incubation of α-amylase with Na+ and Zn2+ ions enhanced/activate the enzyme activity correspondingly, Al3+ and K+ ions exhibited varied degree of inhibition while Ca2+ and Hg2+ ions caused total inhibition on α-amylase activity. The ability of purified α-amylase from Bacillus subtilis under wide range of temperatures and pH suggests its applications in industries and bioremediation of effluent discharge on food processing sites.

Keywords: Bacillus subtilis ; Cassava processing site; α-amylase; Purification; Characterization

Citation: Gbenga A, David S, Femi B, Saanu AB (2017) Purification and Characterization of α-Amylase from Bacillus subtilis Isolated from Cassava Processing Sites. J Bioremediat Biodegrad 8:417 Doi: 10.4172/2155-6199.1000417

Copyright: © 2017 Gbenga A, 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.<

Top