Purification and characterization of antifungal proteins in triticale seed / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 561-565, 2002.
Artículo
en Chino
| WPRIM
| ID: wpr-256164
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.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Farmacología
/
Proteínas de Plantas
/
Semillas
/
Trichoderma
/
Triticum
/
Química
/
Quitinasas
/
Beta-Glucosidasa
/
Glucano 1,3-beta-Glucosidasa
/
Microbiología
Idioma:
Chino
Revista:
Chinese Journal of Biotechnology
Año:
2002
Tipo del documento:
Artículo
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