NISCAIR Online Periodicals Repository

Research Journals >
Indian Journal of Biochemistry and Biophysics (IJBB) >
IJBB Vol.46 [2009] >
IJBB Vol.46(5) [October 2009] >

Title: Partial purification and some properties of -amylase from Bacillus subtilis KIBGE-HAS
Authors: Bano, Saeeda
Qader, Shah Ali Ul
Aman, Afsheen
Azhar, Abid
Keywords: -Amylase
Bacillus sp.
Metal ions
Thermal stability
Issue Date: Oct-2009
Publisher: CSIR
Abstract:  An extracellular -amylase from Bacillus subtilis KIBGE-HAS was partially purified by ultrafiltration and ammonium sulphate precipitation with 19.2-fold purification and specific activity of 4195 U/mg. The enzyme showed relatively high thermostability and retained 62% of its activity when kept at 70°C for 15 min. -Amylase was highly stable at -18°C and loss of activity was very low during stability study. Metal ions like Mn2+, Ca2+, Co2+, K+, Mg2+, and Fe3+ activated the enzyme, while Hg2+ Ba2+, Cu2+, Na+ and Al3+ strongly inhibited the activity. The α-amylase was highly stable in various surfactants and detergents. In the presence of surfactants such as SDS and Triton X-100 the enzyme activity was found 2.9 and 1.8-fold higher respectively than control. The non-ionic detergents (Tween 20 and Tween 80) exhibited slightly inhibitory effect on the enzyme activity.
Page(s): 401-404
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Source:IJBB Vol.46(5) [October 2009]

Files in This Item:

File Description SizeFormat
IJBB 46(5) 401-404.pdf258.9 kBAdobe PDFView/Open
 Current Page Visits: 88 
Recommend this item


Online Submission of Articles |  NISCAIR Website |  National Knowledge Resources Consortium |  Contact us |  Feedback

Disclaimer: NISCAIR assumes no responsibility for the statements and opinions advanced by contributors. The editorial staff in its work of examining papers received for publication is helped, in an honorary capacity, by many distinguished engineers and scientists.

CC License Except where otherwise noted, the Articles on this site are licensed under Creative Commons License: CC Attribution-Noncommercial-No Derivative Works 2.5 India

Copyright © 2015 The Council of Scientific and Industrial Research, New Delhi. All rights reserved.

Powered by DSpace Copyright © 2002-2007 MIT and Hewlett-Packard | Compliant to OAI-PMH V 2.0

Home Page Total Visits: 165285 since 01-Sep-2015  Last updated on 27-Jun-2016Webmaster: