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Kinetic Study and Characterization of 1,4-β-Endoglucanase of Aspergillus niger ANL301

Chinedu, Shalom Nwodo and Nwinyi, Obinna and Okafor, Uzoma A. and Okochi, Veronica I. (2011) Kinetic Study and Characterization of 1,4-β-Endoglucanase of Aspergillus niger ANL301. Dynamic Biochemistry, Process Biotechnology and Molecular Biology, 5 (2). pp. 41-46. ISSN ISSN: 1749-0626

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Abstract

Submerged fermentation of Aspergillus niger ANL 301 in basal medium containing cellulose as sole carbon source, yielded crude extracellular proteins with 0.54 ± 0.02 units mg protein-1 of 1,4-β-endoglucanase activity. Partial purification by ammonium sulphate precipitation (80% saturation) and gel filtration on Sephadex 25-300 gave two active fractions of 1,4-β-endoglucanase, which exhibited close activity towards carboxymethyl-cellulose (CMC). The pH profile of the pooled enzyme fractions showed three activity peaks at pH 3.5, 5.5 and 7.0. The enzyme was most active at pH 5.5 and showed optimal activity at 50°C. Vmax of 4.4 ± 0.4 µmol min-1 mg protein-1 and Km of 12.5 ± 0.4 gL-1 was obtained with CMC for the enzyme. Different divalent metal ions and EDTA affected the enzyme activity at 2.0 mM concentrations in different ways. Mn2+ and Fe2+ exhibited 253.4 and 24.0% stimulatory effects, respectively on the enzyme activity. Mg2+, Ca2+, Cu2+, and Zn2+ inhibited the enzyme by between 22.3 and 29.4%, whereas 75.0 and 71.3% inhibition were obtained with Hg2+ and EDTA, respectively. Manganese ion showed an exceptional activation of the 1,4-β-endoglucanase. The organism produced two types of 1,4-β-endoglucanase with different molecular weights.

Item Type: Article
Uncontrolled Keywords: Aspergillus niger ANL 301, carbon source, carboxymethyl-cellulose (CMC), 1,4-β-endoglucanase activity, kinetics, manganese ion
Subjects: Q Science > Q Science (General)
Divisions: UNSPECIFIED
Depositing User: Dr Shalom N. Chinedu
Date Deposited: 10 Nov 2011 12:22
Last Modified: 14 Nov 2012 11:17
URI: http://eprints.covenantuniversity.edu.ng/id/eprint/543

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