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A comparative study on depolymerization of chitosan by proteolytic enzymes.

Vishu Kumar, A. B. and Tharanathan, R. N. (2004) A comparative study on depolymerization of chitosan by proteolytic enzymes. Carbohydrate Polymers, 58 (3). pp. 275-283.

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Proteolytic enzymes such as pepsin, papain and pronase caused depolymerization of chitosan, a co-polysaccharide of glucosamine and N-acetyl glucosamine residues linked by b-1,4-glycosidic bonds. The pH optima of these enzymes towards chitosanolysis were different from that towards their own substrates, indicating the involvement of pH-sensitive conformational changes during specific and non-specific activities. The depolymerization reaction obeyed Michaelis-Menten kinetics and Km and Vmax values indicated higher affinity of pepsin towards chitosan. The chitosanolytic products were low molecular weight chitosans (LMWC, a major product), chitooligomers (COs) as well as monomers. Low molecular weight chitosans had molecular weight in the range, 4.1–10.0 kDa depending on the reaction time. FT-IR indicated a decrease in the degree of acetylation of LMWC. GPC and HPLC of COs showed a degree of polymerization of 2–8 with a preponderance of di- to hexamer including monomers.

Item Type: Article
Uncontrolled Keywords: Chitosanolysis; Proteases; Non-specificity; Low molecular weight chitosans; Chitooligomers
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 05 Enzymes
600 Technology > 08 Food technology > 28 Meat, Fish & Poultry
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 20 Nov 2008 09:56
Last Modified: 28 Dec 2011 09:40
URI: http://ir.cftri.com/id/eprint/2451

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