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Chitosanolysis by a pectinase isozyme of Aspergillus niger - a non-specific activity

Kittur, F. S. and Vishu Kumar, A. B. and Lalitha, R. Gowda and Tharanathan, R. N. (2003) Chitosanolysis by a pectinase isozyme of Aspergillus niger - a non-specific activity. Carbohydrate Polymers, 53 (2). pp. 191-196.

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Abstract

An isozyme of Aspergillus niger pectinase could depolymerize chitosan and its derivatives. The isozyme showed optimum depolymerization at pH 3.0 and 47 8C and exhibited classical Michaelis–Menten kinetics with a Km and a Vmax of 3.12 mg ml21 and 153.85 nmol min21 mg21, respectively, towards chitosan, which were higher than those for chitosan derivatives. The low molecular weight chitosans (LMWC) obtained were in the range of 6–20 kDa depending on the reaction conditions. Identification of glucosamine (GlcN) and N-acetylglucosamine (GlcNAc) oligomers as depolymerized products indicated that the isozyme cleaved both GlcN-GlcN and GlcNAc- GlcN linkages. This study suggests the possible use of pectinase isozyme in place of chitosanase, which is expensive and unavailable in bulk quantity for the production of LMWC and chitooligomers

Item Type: Article
Uncontrolled Keywords: Chitosan; Pectinase; Low molecular weight chitosans; Chitooligomers
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
Divisions: Protein Chemistry and Technology
Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 22 Jun 2009 07:12
Last Modified: 28 Dec 2011 09:44
URI: http://ir.cftri.com/id/eprint/3449

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