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Porcine Pancreatic alpha-Amylase and its Isoforms: Purification and Kinetic Studies

Anitha, Gopal B. and Muralikrishna, G. (2009) Porcine Pancreatic alpha-Amylase and its Isoforms: Purification and Kinetic Studies. International Journal of Food Properties, 12 (3). 571 -586.

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Official URL: http://dx.doi.org/10.1080/10942910801947755

Abstract

Porcine pancreatic alpha-amylase was separated on DEAE-cellulose into two isoforms, i.e., PPA-I and PPA-II and their molecular weight was found to be ∼ 55 kDa by gel filtration. The pH and temperature optima of PPA and its isoforms were 6.9 and 45°C. Chlorides of metal ions Ca2+, Ba2+, Co2+, and Mg2+ enhanced the enzyme activity, whereas Al3+ and Hg2+ completely inactivated the enzyme. Oxalic and citric acids inhibition of PPA and its isoforms is concentration dependant. EDTA was found to be the most effective inhibitor. PPA and its isoforms released maltotriose and maltotetraose from starches.

Item Type: Article
Uncontrolled Keywords: Porcine pancreatic alpha-amylase was separated on DEAE-cellulose into two isoforms, i.e., PPA-I and PPA-II and their molecular weight was found to be ∼ 55 kDa by gel filtration. The pH and temperature optima of PPA and its isoforms were 6.9 and 45°C. Chlorides of metal ions Ca2+, Ba2+, Co2+, and Mg2+ enhanced the enzyme activity, whereas Al3+ and Hg2+ completely inactivated the enzyme. Oxalic and citric acids inhibition of PPA and its isoforms is concentration dependant. EDTA was found to be the most effective inhibitor. PPA and its isoforms released maltotriose and maltotetraose from starches.
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 16 Protein Biochemistry
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 09 Mar 2010 06:29
Last Modified: 18 Nov 2016 08:16
URI: http://ir.cftri.com/id/eprint/9376

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