Effect of enzymolysis combined with Maillard reaction treatment on functional and structural properties of gluten protein.

In this work, the modified gluten was prepared by enzymolysis combined with Maillard reaction (MEG), and its functional and structural properties were investigated. The result showed that the maximum foamability of MEG was 19.58 m/g, the foam stability was increased by 1.8 times compared with gluten, and the solubility and degree of graft were increased to 44.4 % and 28.1 % at 100 °C, whereas the content of sulfhydryl group decreased to 0.81 μmol/g. The scavenging ability on ABTSradical and DPPH radical of MEG was positively correlated with reaction temperature, and the maximum values were 86.57 % and 71.71 % at 140 °C, respectively. Furthermore, the fluorescence quenching effect of tryptophan and tyrosine residues was enhanced, while the fluorescence intensity decreased with the temperature increase. Scanning electron microscopy revealed that the surface of enzymatically hydrolyzed-gluten became smooth and the cross section became straightened, while MEG turned smaller and irregular approaching a circular structure. FT-IR spectroscopy showed that enzymatic hydrolysis promoted the occurrence of more carbonyl ammonia reactions and the formation of precursors of advanced glycosylation end products. These results provide a feasible method for improving the structure and functional properties of gluten protein.