Interactions between
gluten proteins and water-extractable arabinoxylan
(WEAX) during the heating stage are crucial for the organoleptic quality
of high-fiber cereal products. To reveal the molecular mechanism of
WEAX on gluten characteristic upon heating, the current study comparatively
investigated the effects of WEAX with different molecular weights
(M
w) on the heat-evoked conformational
variation and polymerization behavior of gluten. Results showed that
WEAX, especially low M
w WEAX (L-WEAX),
facilitated the polymerization ability of α-/γ-gliadins
into glutenins, whereas high M
w WEAX (H-WEAX)
reduced the polymerizing temperature of glutenin and gliadin. L-WEAX
could develop more hydrogen bonds with tyrosine of gluten and stabilize
the secondary structure more evidently than H-WEAX upon heating. Compared
with disulfide bridge formation, hydrophobic interactions were not
the driving force involved in the heat-induced polymerization behavior
affected by WEAX. WEAX evoked the reinforced glutenin network and
heterogeneous distribution of gliadin, with a more uniform molecular
surface developed for gluten.
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