Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/731
Title: Biochemical characterization of raw-starch-digesting alpha amylase purified from bacillus amyloliquefaciens
Authors: Dhanya, G
Nampoothiri, K M
Swetha, S
Pandey, A
Keywords: Ion exchange chromatography
Submerged fermentation
Acid reagent
Bacillus amyloliquefaciens
Purification
Raw starch digestion
Alpha amylase
Issue Date: 2009
Publisher: Humana Press
Citation: Applied Biochemistry and Biotechnology 158(3):653-662;Sep 2009
Abstract: Alpha amylase (E.C. 3.2.1.1) of Bacillus amyloliquefaciens produced by submerged fermentation was purified to near homogeneity by ion exchange chromatography. Through the process 38.6-fold increase in purity with a specific activity of 72 U/mg proteins was obtained. The apparent molecular weight of the purified enzyme was found to be 58 kDa by SDS-PAGE. The enzyme was relatively stable between pH 5.0-8.0 and temperature between 50 and 60 degrees'C. The enzyme did not show any obligate requirement of metal ions but Ca(2+) and Cu(2+) enhanced the enzyme activity marginally and the thermostability was enhanced in the presence of Ca(2+) ions. The purified enzyme exhibited maximal substrate specificity for amylose and efficiency in digesting various raw starches. The K(m) and V(max) of the enzyme was determined using both amylose and soluble starch as substrate. The analysis of the hydrolyzed products of soluble starch by thin layer chromatography showed the yield of maltosaccharides after 6 h of hydrolysis.
URI: http://ir.niist.res.in:8080/jspui/handle/123456789/731
ISSN: 0273-2289
Appears in Collections:2009

Files in This Item:
File Description SizeFormat 
2009 _ 00030.pdf156.62 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.