4.7 Article

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

Journal

FOOD HYDROCOLLOIDS
Volume 134, Issue -, Pages -

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2022.108046

Keywords

Arabinoxylan; Feruloylation; Heat-evoked; Gluten; Polymerization behavior

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This study investigated the role of feruloylation of arabinoxylan (AX) in regulating the heat-evoked polymerization behavior of gluten. The results showed that AX enhanced the polymerization degree of glutenin-glutenin and glutenin-gliadin crosslinks, while ferulic acid (FA) suppressed the polymerization behavior compared to AX free of FA. The study also demonstrated that AX with the highest FA level exhibited the optimum elevation effect on the viscoelasticity of gluten. These findings provide valuable insights into the interaction mechanism between AX and gluten proteins, and could contribute to the development of nutritious high-fiber wheat-based products with superior organoleptic quality.
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 polymeri-zation 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 alpha/gamma-gliadins in glutenin-gliadin crosslinks. The complete polymerization of glutenin and gliadin elevated the intermolecular 13-sheet and ordered alpha-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 nutri-tious high-fiber wheat-based products with superior organoleptic quality.

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