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生物工程学报 2002
Purification and Characterization of Antifungal Proteins in Triticale Seed
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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.