A Reducing-End-Acting Chitinase From Vibrio Proteolyticus Belonging to Glycoside Hydrolase Family 19

Appl Microbiol Biotechnol. 2008 Mar;78(4):627-34. doi: 10.1007/s00253-008-1352-2. Epub 2008 Jan 23.

Abstract

A chitinase gene belonging to the glycoside hydrolase family 19 from Vibrio proteolyticus (chi19) was cloned. The recombinant enzyme (Chi19) showed weak activities against polymeric substrates and considerable activities against fully N-acetylated chitooligosaccharides, (GlcNAc)(n), whose degree of polymerization was greater than or equal to five. It hydrolyzed (GlcNAc)(n) at the second linkage position from the reducing ends of the chitooligosaccharides. The hydrolytic products of colloidal chitin were mainly (GlcNAc)(2) from the initial stage of the reaction. The hydrolytic pattern of reduced colloidal chitin clearly suggested that the enzyme hydrolyzed the polymeric substrate from the reducing end.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Biopolymers / metabolism
  • Chitin / metabolism
  • Chitinases / chemistry*
  • Chitinases / genetics
  • Chitinases / isolation & purification
  • Chitinases / metabolism*
  • Cloning, Molecular
  • Enzyme Stability
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism
  • Hydrolysis
  • Molecular Sequence Data
  • Multigene Family*
  • Sequence Analysis, DNA
  • Substrate Specificity
  • Vibrio / enzymology*
  • Vibrio / genetics

Substances

  • Bacterial Proteins
  • Biopolymers
  • Chitin
  • Glycoside Hydrolases
  • Chitinases

Associated data

  • GENBANK/AB253418