[Purification and characterization of antifungal proteins in triticale seed].
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.
Na
Bing
B
Graduate School, University of Science and Technology of China, Beijing 100039, China.
Yu
Ming-Kun
MK
Gong
Jun
J
Wu
Jin
J
D000935:Antifungal Agents / Q000302:isolation & purification* / Q000494:pharmacology; D002688:Chitinases / Q000302:isolation & purification* / Q000494:pharmacology; D043326:Glucan 1,3-beta-Glucosidase; D008970:Molecular Weight; D010940:Plant Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D012639:Seeds / Q000737:chemistry*; D014242:Trichoderma / Q000187:drug effects*; D014908:Triticum / Q000737:chemistry* / Q000382:microbiology; D001617:beta-Glucosidase / Q000302:isolation & purification* / Q000494:pharmacology
D000935:Antifungal Agents; D010940:Plant Proteins; D002688:Chitinases; D001617:beta-Glucosidase; D043326:Glucan 1,3-beta-Glucosidase