The role of feruloylation of wheat bran arabinoxylan in regulating the heat-evoked polymerization behavior of gluten

Abstract

To further reveal the role of feruloylation of arabinoxylan (AX) in regulating the heat-evoked polymerization behavior of gluten, AX was extracted from wheat bran and in situ modified with lime to obtain AX with controlled ferulic acid (FA) content. The effects of AX with varied FA level on the heat-evoked polymerization of gluten were comparatively studied. The results suggested that AX postponed the disulfide bond mediated polymerization behavior of glutenins and enhanced polymerization degree of glutenin-glutenin and glutenin-gliadin crosslinks upon thermal treatment, while FA moiety suppressed the facilitated polymerization behavior compared with AX free of FA. iTARQ analysis demonstrated that FA moiety of AX mainly suppressed the polymerization of low molecular weight glutenin subunits and α/γ-gliadins in glutenin-gliadin crosslinks. The complete polymerization of glutenin and gliadin elevated the intermolecular β-sheet and ordered α-helix structures at the expense of other structures, while AX stabilized the transformation of secondary structures and was irrelevant with FA level. FA moiety of AX contributed to stabilizing the microenvironment of tryptophan, and evoked the disulfide bond conformation with reduced gauche-gauche-gauche conformation upon formation of glutenin-gliadin crosslinks. AX with the highest FA level exhibited the optimum elevation effect on the viscoelasticity of gluten, which might be attributed to the moderate polymerization of glutenin-gliadin and potential covalent linkage formed between the FA moiety of AX and gluten. This study could contribute to depicting the interacting mechanism of AX and gluten proteins, and further provide basis for exploiting nutritious high-fiber wheat-based products with superior organoleptic quality. • Arabinoxylan (AX) was in situ modified to control the ferulic acid (FA) content. • FA of AX contributed to suppressing the heat-evoked polymerization of gluten proteins. • Suppressed polymerized subunits of gluten upon heating by FA were identified. • FA moiety of AX contributed to stabilizing the microenvironment of tryptophan. • AX with high FA level exhibit optimum elevation effect on viscoelasticity of gluten.