Purification and characterization of a chitinase from Bombyx mori.
- Author:
Mingyan LIU
1
;
Hongbin ZHANG
;
Xueqin HU
;
Qingli WEI
Author Information
1. Department of Pharmaceutical Engineering, Hefei University of Technology, Hefei 230009, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Bombyx;
enzymology;
Chitinases;
isolation & purification;
metabolism;
Enzyme Stability;
Insect Proteins;
isolation & purification;
metabolism;
Temperature
- From:
Chinese Journal of Biotechnology
2010;26(3):404-409
- CountryChina
- Language:Chinese
-
Abstract:
The importance of chitinases in the physiological and developmental processes of fungi and insects makes themselves and their inhibitors important targets for biological pesticides. A chitinase was isolated from Bombyx mori and purified to electrophoretic homogeneity by ammonium sulfate precipitation and Sephadex G-150 column chromatography. The molecular mass was estimated to be about 88 kDa by SDS-PAGE, while the K(m) was calculated to be 22.3 micromol/L. Moveover, the optimal reaction temperature was 45 degrees C, and the optimum pH was 6.0. The effect of metal ions and organic reagents on chitinase activity was investigated. The activity was enhanced by high concentration of Mn2+, while was strongly inhibited by Cu2+ and SDS. These results provide a basis for screening the chitinase-based biological pesticide.
