Chitinase A From Stenotrophomonas Maltophilia Shows Transglycosylation and Antifungal Activities

Bioresour Technol. 2013 Apr;133:213-20. doi: 10.1016/j.biortech.2013.01.103. Epub 2013 Jan 29.

Abstract

Stenotrophomonas maltophilia chitinase (StmChiA and StmChiB) genes were cloned and expressed as soluble proteins of 70.5 and 41.6 kDa in Escherichia coli. Ni-NTA affinity purified StmChiA and StmChiB were optimally active at pH 5.0 and 7.0, respectively and exhibited broad range pH activity. StmChiA and StmChiB had an optimum temperature of 40°C and are stable up to 50 and 40°C, respectively. Hydrolytic activity on chitooligosaccharides indicated that StmChiA was an endo-acting enzyme releasing chitobiose and StmChiB was both exo/endo-acting enzyme with the release of GlcNAc as the final product. StmChiA showed higher preference to β-chitin and exhibited transglycosylation on even chain length tetra- and hexameric substrates. StmChiA, and not StmChiB, was active on chitinous polymers and showed antifungal activity against Fusarium oxysporum.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antifungal Agents / pharmacology*
  • Chitin / metabolism
  • Chitinases / chemistry
  • Chitinases / isolation & purification
  • Chitinases / metabolism*
  • Chitinases / ultrastructure
  • Cloning, Molecular
  • Enzyme Stability / drug effects
  • Fungi / drug effects
  • Glycosylation / drug effects
  • Hydrogen-Ion Concentration / drug effects
  • Hydrolysis / drug effects
  • Kinetics
  • Microbial Sensitivity Tests
  • Protein Structure, Tertiary
  • Sequence Analysis, Protein
  • Solubility
  • Stenotrophomonas maltophilia / enzymology*
  • Substrate Specificity / drug effects
  • Temperature
  • Time Factors

Substances

  • Antifungal Agents
  • Chitin
  • Chitinases