Purification and Characterization of a Protease Inhibitor from Fagopyrum tartaricum Gaertn Seeds and Its Effectiveness Against Insects
- VernacularTitle:一种苦荞麦种子蛋白酶抑制剂的纯化、特性及其抗虫活性
- Author:
Zhuanhua WANG
;
Zhuohui ZHAO
;
Zheng ZHANG
;
Jingming YUAN
;
Dan NOBACK
;
Gunilla WIESLANDER
- Publication Type:Journal Article
- Keywords:
tartary buckwheat ( Fagopyrum tartaricum Gaertn);
trypsin inhibitor;
purification;
anti-insect activity
- From:
Chinese Journal of Biochemistry and Molecular Biology
2006;22(12):960-965
- CountryChina
- Language:Chinese
-
Abstract:
Protease inhibitors, which are widely distributed in all types of life forms, are generally considered to be one of the most abundant proteins and a defense mechanism. A protease inhibitor from tartary buckwheat seeds (TBTI-Ⅱ ), with specific trypsin-inhibitory activity, was obtained by Resource Q anion-exchange chromatography and Superdex G 75 gel filtration. SDS-PAGE analysis indicated that the approximate molecular weight was 9.0 kD. Amino-acid analysis showed that the TBTI- Ⅱ was composed of 80 amino-acid residues with a high content of glutamate, aspartate and arginine. The inhibitor had high thermostability and retained 67.6% of its activity after heating at 100℃ for 10 min. The inhibition constant Ki was determined to be 1.01× 10-4 mol/L. It was demonstrated that the inhibitor was able to have an effect on the growth of cotton bollworm larva, after being fed with the artificial diets mixed with the target inhibitor. The present study indicates that the trypsin inhibitor from tartary buckwheat seeds could be a new potential anti-insect factor.
