小黑麦抗真菌蛋白组分的分离纯化和性质研究  

Purification and Characterization of Antifungal Proteins in Triticale Seed

作　　者：那冰[1] 余明琨[1] 龚隽[1] 吴襟[2] 

机构地区：[1]中国科技大学研究生院,北京100039 [2]中国科学院微生物研究所,北京100080

出　　处：《生物工程学报》2002年第5期561-565,共5页Chinese Journal of Biotechnology

摘　　要：以木霉为指示菌 ,小黑麦中饲 2 37种子中的蛋白提取物经过分离纯化后 ,得到了 3种主要的抗真菌蛋白组分 ,经酶活检测鉴定 ,分别是分子量为 30 .5kD的ClassⅡ型几丁质酶 ,两种分子量为 5 1kD和 2 3kD的 β 1,3 葡聚糖酶。其中几丁质酶的最适反应pH为 6 0 ,最适反应温度为 37℃ ,测定的N 末端氨基酸序列与大麦几丁质酶的有很高的同源性。在一定条件下 ,这 3种蛋白组分都有较强的抗木霉活性 ,并且有明显的协同作用 。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 ClassⅡ chitinase and two kinds of β-1 ,3-glucanases. Chitinase molecular mass was 30.5 kD and enzyme activity was maximal at pH 6.0 and 37℃. Two β-glucanases molecular masses were 51kD and 23kD. N-terminal amino acid sequences of Triticale chitinase share high homology with barley chitinase. In some conditions, the chitinase and β-glucanases all had strong antifungal activity and were able to inhibit Trichoderma growth synergistically. Moreover, the chitinase and β-1,3-glucanases were able to inhibit powdery mildew growth on detached susceptible wheat leaves.

关 键 词：小黑麦 抗真菌蛋白组分 分离纯化 性质 几丁质酶 Β-1 3-葡聚糖酶 

分 类 号：Q946[生物学—植物学]