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Purification and Characterization of Endo-β-1,4 Mannanase from Aspergillus niger gr for Application in Food Processing Industry

Naganagouda, K. and Salimath, P. V. and Mulimani, V. H. (2009) Purification and Characterization of Endo-β-1,4 Mannanase from Aspergillus niger gr for Application in Food Processing Industry. Journal of Microbiology and Biotechnology, 19 (10). pp. 1184-1190.

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J._Microbiol._Biotechnol._(2009),_19(10),_1184–1190.pdf
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Abstract

A thermostable extracellular β-mannanase from the culture supernatant of a fungus Aspergillus niger gr was purified to homogeneity. SDS-PAGE of the purified enzyme showed a single protein band of molecular mass 66 kDa. The β- mannanase exhibited optimum catalytic activity at pH 5.5 and 55oC. It was thermostable at 55oC, and retained 50% activity after 6 h at 55oC. The enzyme was stable at a pH range of 3.0 to 7.0. The metal ions Hg2+, Cu2+, and Ag2+ inhibited complete enzyme activity. The inhibitors tested, EDTA, PMSF, and 1,10-phenanthroline, did not inhibit the enzyme activity. N-Bromosuccinimide completely inhibited enzyme activity. The relative substrate specificity of enzyme towards the various mannans is in the order of locust bean gum>guar gum>copra mannan, with Km of 0.11, 0.28, and 0.33 mg/ml, respectively. Since the enzyme is active over a wide range of pH and temperature, it could find potential use in the food-processing industry.

Item Type: Article
Uncontrolled Keywords: Aspergillus niger gr, food processing, β-mannanase, purification
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology > 04 Fungi
600 Technology > 08 Food technology > 05 Processing and Engineering
500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 28 Polysaccharide Chemistry
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 12 Nov 2010 03:50
Last Modified: 28 Dec 2011 10:19
URI: http://ir.cftri.com/id/eprint/9765

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