The Study Of Catalytic Mechanism Of Transglutaminase On Wheat Protein And Starch

Transglutaminase(TG) as a new, safe enzyme, which has been researched about ten years in foreign country. A series of tests had been carried out and it has gradually applied to the production of flour products, but there is less research about this area in domestic. The present researches of Transglutaminase focused on the two aspects of milling and pasta processing : the use of TG can improve flour quality, extend shelf life and reduce the allergenicity of wheat flour in the processes of tempering and mixing wheat flour, it can also rebound wheat quality when TG was used to hand Worm-eaten wheat and improve food quality of baked goods such as bread, cookies, cakes and so on. Therefore, the use of covalent crosslinking properties of Transglutaminase can improve the flour quality, which has a great significance and foreground in the processing of flour products.In this paper, the catalytic mechanism of TG in and between the components of wheat protein and starch granules was researched, meanwhile, the effort of group structure of wheat and buckwheat noodles was discussed, all above have laid a theoretical foundation for the development of flour processing.Through this research, the main conclusions were as following:(1)Based on the method of components separation,wheat albumin, globulin, gliadin, glutenin and starch granules were obtained, the effect of transglutaminase on the intra- and interaction of these isolated compounds was studied in the paper. The reaction was studied at the levels of single, two, three and four kinds of protein compounds and starch granules. Before and after the enzymatic reaction, content and molecular weight were analyzed according to the soluble protein content and SDS-PAGE analysis, and microstructure of the starch granules was also observed by using EMS. The results showed that TG could catalyze the interactions inner a same protein or between the different proteins including albumin, globulin, and gliadin. The effect of TG was greater on globulin than on albumin, and the greatest on gliadin among the three proteins. Albumin showed a negative effect on TG catalyzing the interaction of globulin and gliadin, while globulin showed a negative effect on gliadin.(2)Meanwhile, The Soba and the mixture of buckwheat flour and wheat were used as the control group to research the effect of transglutaminase (TGase) on the interaction among the buckwheat and wheat protein compounds in the aspects of microstructure, soluble protein content, and protein compounds. Results showed that TG strengthened the structure of gluten net in dough of wheat, buckwheat and mixture of the both. TG also could catalyze the interaction of albumin and globulin of wheat and buckwheat. As to buckwheat, the effect of TG was greater on albumin than on globulin, however, for wheat, it was reverse. TG showed greater effect on the mixture of buckwheat albumin and globulin than wheat albumin and globulin.