A chitinase with antifungal activity from the mung bean

Protein Expr Purif. 2005 Apr;40(2):230-6. doi: 10.1016/j.pep.2004.06.032.


A chitinase with antifungal activity was isolated from mung bean (Phaseolus mungo) seeds. The procedure entailed aqueous extraction, (NH4)2SO4 precipitation, ion-exchange chromatography on CM-Sepharose, high-performance liquid chromatography (HPLC) on Poros HS-20, and gel filtration on Sephadex G-75. The protein exhibited a molecular mass of 30.8 kDa in SDS-polyacrylamide gel electrophoresis. Its pI was 6.3 as determined by isoelectric focusing. The specific activity of the chitinase was estimated to be 3.81 U/mg. The enzyme expressed its optimum activity at pH 5.4 and was stable from 40 to 50 degrees C. It exerted antifungal action toward Fusarium solani, Fusarium oxysporum, Mycosphaerella arachidicola, Pythium aphanidermatum, and Sclerotium rolfsii.

MeSH terms

  • Antifungal Agents / isolation & purification*
  • Antifungal Agents / pharmacology
  • Chemical Fractionation
  • Chitinases / isolation & purification
  • Chitinases / pharmacology*
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Fabaceae / enzymology*
  • Fusarium / drug effects
  • Hydrogen-Ion Concentration
  • Mitosporic Fungi / drug effects*
  • Pythium / drug effects
  • Seeds / enzymology
  • Temperature


  • Antifungal Agents
  • Chitinases