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Molecules. 2013 Mar 4;18(3):2978-87. doi: 10.3390/molecules18032978.

The identification and characterization of chitotriosidase activity in pancreatin from porcine pancreas.

Author information

  • 1Department of Medical Biotechnology and Laboratory Science, College of Medicine, Chang Gung University, 259 Wen-Hwa 1st Road, Kweishan, Taoyuan 33302, Taiwan. crshen@mail.cgu.edu.tw

Abstract

The versatile oligosaccharide biopolymers, chitin and chitosan, are typically produced using enzymatic processes. However, these processes are usually costly because chitinases and chitosanases are available in limited quantities. Fortunately, a number of commercial enzymes can hydrolyze chitin and chitosan to produce long chain chitin or chitosan oligosaccharides. Here, a platform to screen for enzymes with chitinase and chitosanase activities using a single gel with glycol chitin or glycol chitosan as a substrate was applied. SDS-resistant chitinase and chitosanase activities were observed for pancreatin. Its chitotriosidase had an optimal hydrolysis pH of 4 in the substrate specificity assay. This activity was thermally unstable, but independent of 2-mercaptoethanol. This is the first time a chitotriosidase has been identified in the hog. This finding suggests that oligochitosaccharides can be mass-produced inexpensively using pancreatin.

PMID:
23459306
[PubMed - indexed for MEDLINE]
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