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

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

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chitin / chemistry
  • Chitosan / chemistry
  • Hexosaminidases / metabolism*
  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Pancreas / chemistry*
  • Pancreas / enzymology*
  • Pancreatin / metabolism*
  • Substrate Specificity
  • Swine

Substances

  • Chitin
  • Pancreatin
  • Chitosan
  • Hexosaminidases
  • chitotriosidase