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Non-specific depolymerization of chitosan by pronase and characterization of the resultant products

Vishu Kumar, Acharya B and Gowda, Lalitha R. and Tharanathan, R. N. (2004) Non-specific depolymerization of chitosan by pronase and characterization of the resultant products. European Journal of Biochemistry, 271. pp. 713-723.

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Pronase (type XXV serine protease from Streptomyces griseus) efficiently depolymerizes chitosan, a linear bfi1,4-linked polysaccharide of 2-amino-deoxyglucose and 2-amino-2-N-acetylamino-D-glucose, to low-molecular weight chitosans (LMWC), chito-oligomers (degree of polymerization,2–6) and monomer. The maximum depolymerization occurred at pH 3.5 and 37°C,and there action obeyed Michaelis–Menten kinetics with a Km of 5.21 mgmL-1)1 and Vmax of 138.55 nmolesmin-1mg-1. The molecular mass of the major product, LMWC, varied between 9.0 ± 0.5 kDa depending on the reaction time. Scanning electron microscopy of LMWC showed an approximately eightfold decrease in particle size and characterization by infrared spectroscopy, circular dichroism, X-ray diffractometry and 13C-NMR revealed them to possess a lower degree of acetylation, hydration and crystallinity compared to chitosan. Chitosanolysis by pronase is an alternative and inexpensive method to produce a variety of chitosan degradation products that have wide and varied biofunctionalities.

Item Type: Article
Uncontrolled Keywords: chitosan; chito-oligomers; low-molecular weight chitosan; pronase; structure.
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology > 07 Enzyme Biochemistry
600 Technology > 08 Food technology > 28 Meat, Fish & Poultry
Divisions: Dept. of Biochemistry
Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 26 Jun 2007 09:21
Last Modified: 28 Aug 2018 06:05
URI: http://ir.cftri.com/id/eprint/1269

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