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Non-specific depolymerization of chitosan by pronase and characterization of the resultant products
Article first published online: 26 JAN 2004
DOI: 10.1111/j.1432-1033.2003.03975.x
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How to Cite
Kumar, A. B. V., Gowda, L. R. and Tharanathan, R. N. (2004), Non-specific depolymerization of chitosan by pronase and characterization of the resultant products. European Journal of Biochemistry, 271: 713–723. doi: 10.1111/j.1432-1033.2003.03975.x
Publication History
- Issue published online: 26 JAN 2004
- Article first published online: 26 JAN 2004
- (Received 30 October 2003, revised 12 December 2003, accepted 22 December 2003)
- Abstract
- Article
- References
- Cited By
Keywords:
- chitosan;
- chito-oligomers;
- low-molecular weight chitosan;
- pronase;
- structure
Pronase (type XXV serine protease from Streptomyces griseus) efficiently depolymerizes chitosan, a linear β→1,4-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 the reaction obeyed Michaelis–Menten kinetics with a Km of 5.21 mg·mL−1 and Vmax of 138.55 nmoles·min−1·mg−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.