Original scientific paper

Purification and Biochemical Characterization of pH Tolerant and Acid Stable á-amylase from Aspergillus oryzae JGI 21 Isolated from Soil

KN Varalakshmi ; Department of Biotechnology, Centre for Post-GraduateStudies, JainUniversity, 18/3, 9th Main, III Block, Jayanagar, Bangalore – 560 011
Bablee Tamrakar ; Department of Biotechnology, Centre for Post-GraduateStudies, JainUniversity, 18/3, 9th Main, III Block, Jayanagar, Bangalore – 560 011
Kusum Kumari ; Department of Biotechnology, Centre for Post-GraduateStudies, JainUniversity, 18/3, 9th Main, III Block, Jayanagar, Bangalore – 560 011
Priti Kumari ; Department of Biotechnology, Centre for Post-GraduateStudies, JainUniversity, 18/3, 9th Main, III Block, Jayanagar, Bangalore – 560 011
Shreya Navale ; Department of Biotechnology, Centre for Post-GraduateStudies, JainUniversity, 18/3, 9th Main, III Block, Jayanagar, Bangalore – 560 011
Sushil Pokhrel ; Department of Biotechnology, Centre for Post-GraduateStudies, JainUniversity, 18/3, 9th Main, III Block, Jayanagar, Bangalore – 560 011

Abstract

This paper describes the purification and characterization of a novel acid stable and pH tolerant α-amylase from a Aspergillusoryzae JGI
21 isolated from Mangalore. The enzyme displayed a molecular weight of 22 kDa and it was stable over a broad range of acidic and alkaline pH with maximum activity and stability at 6.5. The optimum temperature of enzyme stability was found to be around 24+/-2◦C. The purification of α-amylase by ammonium sulphate precipitation and ion-exchange chromatography resulted in 23.56 fold increase in its activity (100.38 U/mg protein). Considering its promising properties, this enzyme can find potential applications in the food industry as well as in laundry detergents.

Keywords

Aspergillus oryzae JGI 21; acidophilic á-amylase; pH stability; purification; solid-state fermentation

Hrčak ID:

105653

URI

https://hrcak.srce.hr/105653

Publication date:

30.6.2013.

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