African Journal of
Microbiology Research

  • Abbreviation: Afr. J. Microbiol. Res.
  • Language: English
  • ISSN: 1996-0808
  • DOI: 10.5897/AJMR
  • Start Year: 2007
  • Published Articles: 5232

Full Length Research Paper

Purification and characterization of chitinase from Gliocladium catenulatum strain HL-1-1

Gui-Zhen Ma1*, Hui-Lan Gao2, Yong-Hua Zhang2, Shi-Dong Li2, Bing-Yan Xie3 and Sheng-Jun Wu1      
1Huaihai Institute of Technology, Lianyungang, 222005, China. 2Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, 100081 China. 3Institute of Vegetable and Flower, Chinese Academy of Agricultural Sciences (CAAS), Beijing 100081, China.  
Email: [email protected]

  •  Accepted: 30 March 2012
  •  Published: 30 May 2012


Chitinase was isolated and purified from Gliocladium catenulatum through ammonium sulfate sedimentation, sephadex G-25 gel filtration, deionization, ultra filtration condensation, negative ion exchange separation, and non-denaturing gel electrophoresis. A 51 kDa chitinase was purified from the fungus through sodium dodecyl sulfate polyacrylamide gel electrophoresis. The optimum temperature and pH for chitinase activity were 60°C and pH 6.0, respectively. The enzyme solution was stable from 20 to 40°C and pH 4 to 5. Co2+ and Ca2+ were conducive to the enzyme activity, whereas the Fe3+, Cu2+, and Ag+ evidently inhibited the enzyme activity. Fe2+, Na+, K+, Zn2+, and Mn2+ showed less inhibitory effects on the enzyme activity. The Km of the chitinase was 2.832 mg ml-1. The chitanase were found to inhibit the hyphal growth, conidial germination and sclerotial germination of various plant pathogenic fungi.


Key words: Gliocladium catenulatum, chitinases, purification, characteristics.