Production, purification, and characterization of two extremely halotolerant, thermostable, and alkali-stable [alpha]-amylases from Chromohalobacter sp. TVSP 101

Prakash, B. and Vidyasagar, M. and Madhukumar, M. S. and Muralikrishna, G. and Sreeramulu, K. (2009) Production, purification, and characterization of two extremely halotolerant, thermostable, and alkali-stable [alpha]-amylases from Chromohalobacter sp. TVSP 101. Process Biochemistry, 44 (2). pp. 210-215. ISSN 1359-5113

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Abstract

The halophilic bacterial strain Chromohalobacter sp. TVSP 101 was shown to produce extracellular, halotolerant, alkali-stable and moderately thermophilic [alpha]-amylase activity. The culture conditions for higher amylase production were optimized with respect to NaCl, pH, temperature and substrates. Maximum amylase production was achieved in a medium containing 20% NaCl or 15% KCl at pH 9.0 and 37C in the presence of 0.5% rice flour and tryptone. Addition of 50mM CaCl2 to the medium increased amylase production by 29%. Two kinds of amylase activity, designated amylase I and amylase II, were purified from culture filtrates to homogeneity with molecular masses of 72 and 62kDa, respectively. Both enzymes had maximal activity at pH 9.0 and 65C in the presence of 0-20% (w/v) NaCl but amylase I was much more stable in the absence of NaCl than amylase II. The enzymes efficiently hydrolyzed carbohydrates to yield maltotetraose, maltotriose, maltose, and glucose as the end products.

Item Type:	Article
Uncontrolled Keywords:	Production Halotolerant Alkali-stable [alpha]-amylase Chromohalobacter sp. TVSP 101 Rice flour Purification
Subjects:	500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 07 Enzyme Biochemistry 500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology > 02 Bacteriology
Divisions:	Dept. of Biochemistry
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	17 Jun 2009 11:38
Last Modified:	28 Dec 2011 10:09
URI:	http://ir.cftri.res.in/id/eprint/9062

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