Research progress on the change of sulfhydryl group and disulphide bond in wheat gluten protein during processing of flour products
Disulphide bond (S-S) is the most important covalent bond in wheat gluten protein,enhancing the compactness of the spatial structure of protein peptide chains. Under certain conditions,S-S can be converted into sulfhydryl group (-SH). This paper reviewed recent domestic and international research on the changes of-SH and S-S in the processing of flour products elucidating the mechanisms of-SH and S-S in changing the network structure of gluten protein. The transforming mechanisms of-SH and S-S in wheat gluten protein in the processing of flour products were discussed from two aspects:processing conditions (temperature change,non-thermal processing technology) and additives (salts,proteins,enzymes,oxidants,reducing agents,and sulfhydryl blocking agents). It was believed that the formation of S-S in wheat gluten protein usually involves two pathways:-SH oxidation and-SH/S-S exchange reaction. Low temperature conditions such as refrigeration and freezing could increase the free-SH content of the system,leading to a decrease in the firmness of the gluten protein network. Moderate high temperature,high pressure,mechanical external force,vacuum and other conditions could promote protein cross-linking through S-S,which was conducive to the formation of the gluten protein network. External additives could alter the exchange reaction of-SH and S-S in gluten proteins. The moderate potassium salts,wheat protein disulfide isomerases,reducing agents,and thiol blocking agents could interfere with the conversion of free-SH to S-S,thereby slowing down the formation of S-S in gluten proteins. The moderate sodium salts,acidic proteases,oxidases,and oxidants could promote the formation of S-S and three-dimensional polymerization networks. However,current research objects mainly focus on staple flour products such as noodles,and the research on the dynamic molecular structure changes of-SH and S-S during the processing of facial products is limited. In addition,the research on the relationship between natural functional factors and-SH and S-S in gluten protein is also less. In the future,the variety of research objects should be further expanded,and multiple new technologies should be synergistically applied to analyze the dynamic molecular structure of-SH and S-S in gluten protein. More emphasis should be placed on the research and development of functional flour products and the exploration of chemical mechanisms. The review provided theoretical reference for deciphering the mechanism of-SH and S-S in influencing the quality of flour products and explored new research ideas for improving the quality of flour products and breeding special wheat varieties with-SH and S-S as the breakthroughs.
sulfhydryl groupdisulphide bondflour productwheat gluten protein
万方数据
维普
