Purfication And Characteristic Research Of Xylanase Inhibitor From Wheat

We purificated one of kinds of Xylanase inhibitors from wheat(small leaf 22),whose N-terminal amino acid sequence was determined, and investigated the characterizations and the inhibition of the inhibitors.There are four parts in this study:1 A new kind of protein with xylanse inhibit activity was purficated from wheat: taking XynⅢwe get in our own lab and SDS-PAGE electrophoresis as tracking measure,through the methods of salt out, dialysis and ion change chromatogram, the protein is obtained.2 The N-terminal amino acid sequence of the inhibitor was determined:SVSSVVS. There’s no protein with higher sequence homology existing in the Gene Bank after comparison, so the protein is simply determined as a new kind of xylanase inhibiting protein.3 The study on the basic property of the inhibitor shows:the optimum temperature of the protein after combining with xylanase in inhibiting activity is 30℃, and the heat stability is very good until 70℃,. Besides, it possesses no hydrolysing activity towards CMC, Birch xylan, oat xylan and Laminaria.4 Study on the inhibition of the inhibitor shows:The protein can inhibit xylanase in G/11 family but in F/10 family. Moreover, the protein has inhibit activity to xylanase from both bacteria and fungi and also to the cellulose from A.niger,penicillium and cellulase.