Purification and characterization of antifungal proteins in triticale seed.
- Author:
Bing NA
1
;
Ming-Kun YU
;
Jun GONG
;
Jin WU
Author Information
1. Graduate School, University of Science and Technology of China, Beijing 100039, China.
- Publication Type:Journal Article
- MeSH:
Antifungal Agents;
isolation & purification;
pharmacology;
Chitinases;
isolation & purification;
pharmacology;
Glucan 1,3-beta-Glucosidase;
Molecular Weight;
Plant Proteins;
isolation & purification;
pharmacology;
Seeds;
chemistry;
Trichoderma;
drug effects;
Triticum;
chemistry;
microbiology;
beta-Glucosidase;
isolation & purification;
pharmacology
- From:Chinese Journal of Biotechnology
2002;18(5):561-565
- CountryChina
- Language:Chinese
-
Abstract:
Using Trichoderma as an indicative fungus, three antifungal proteins in Triticale Zhongsi 237 seed were purified and characterized. These protein components were considered to be a new Class II chitinase and two kinds of beta-1, 3-glucanases. Chitinase molecular mass was 30.5 kD and enzyme activity was maximal at pH 6.0 and 37 degrees C. Two beta-glucanases molecular masses were 51 kD and 23 kD. N-terminal amino acid sequences of Triticale chitinase share high homology with barley chitinase. In some conditions, the chitinase and beta-glucanases all had strong antifungal activity and were able to inhibit Trichoderma growth synergistically. Moreover, the chitinase and beta-1, 3-glucanases were able to inhibit powdery mildew growth on detached susceptible wheat leaves.
