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

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Relation http://ir.cftri.com/1269/
EJB-01-04
 
Title Non-specific depolymerization of chitosan by pronase
and characterization of the resultant products
 
Creator Vishu Kumar, Acharya B
Gowda, Lalitha R.
Tharanathan, R. N.
 
Subject 07 Enzyme Biochemistry
28 Meat, Fish & Poultry
 
Description 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.
 
Date 2004
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
Identifier http://ir.cftri.com/1269/1/Eur._J._Biochem._271%2C_713-723_%282004%29.pdf
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.