Protein oxidation-induced changes in the aggregation behavior and structure of gluten
Bang‐Bang Li, Zhiyuan Cao, Wei Zhang, Wei Shan, Yangyong Lv, Yuansen Hu
Abstract
Protein oxidation has been proven to affect the rheological characteristics of flour, but the mechanism of protein oxidation on gluten in dough remains unclear. Effect of protein oxidation on the aggregation behavior of gluten in dough was investigated in this study. The results showed that the average diameter of gluten particles of ZM 9023 and YM 15 decreased from 12.96 μm to 3.91 μm–0.68 μm and 0.65 μm respectively after protein oxidation, further research showed that protein oxidation weakenend the aggregation behavior of gluten proteins through destroying disulfide bonds, weakening surface hydrophobicity, increasing electrostatic repulsion and changing the molecular weight distribution of gluten. In addition, atomic force microscopy and confocal laser scanning microscopy images of gluten showed that protein oxidation led to a change in gluten structure. The above results show that protein oxidation affects the aggregation behavior and conformation of gluten by changing its components and crosslinking degree.