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Role of Gluten and Its Components in Determining Durum Semolina Dough Viscoelastic Properties
Author(s) -
Edwards N. M.,
Mulvaney S. J.,
Scanlon M. G.,
Dexter J. E.
Publication year - 2003
Publication title -
cereal chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.558
H-Index - 100
eISSN - 1943-3638
pISSN - 0009-0352
DOI - 10.1094/cchem.2003.80.6.755
Subject(s) - glutenin , gluten , gliadin , chemistry , food science , viscoelasticity , rheology , biochemistry , composite material , materials science , gene , protein subunit
Gluten was isolated from three durum wheat cultivars with a range in strength. Gluten was further fractionated to yield gliadin, glutenin and high molecular weight (HMW) and low molecular weight (LMW) glutenin subunits (GS). The gluten and various fractions were used to enrich a base semolina. Enriched dough samples were prepared at a fixed protein content using a 2‐g micromixograph. Mixing strength increased with addition of gluten. Dynamic and creep compliance responses of doughs enriched with added gluten ranked in order according to the strength of the gluten source. Gliadin addition to dough resulted in weaker mixing curves. Gliadin was unable to form a network structure, having essentially no effect on dough compliance, but it did demonstrate its contribution to the viscous nature of dough (increased tan δ). Source of the gliadin made no difference in response of moduli or compliance. Addition of glutenin to the base semolina increased the overall dough strength properties. Glutenin source did influence both dynamic and compliance results, indicating there were qualitative differences in glutenin among the three cultivars. Enrichment with both HMW‐GS and LMW‐GS increased overall dough strength. Source of HMW‐GS did not affect compliance results; source of LMW‐GS, however, did have an effect. The LMW‐2 proteins strengthened dough to a greater extent than did LMW‐1. Mechanisms responsible for dough viscoelastic properties are described in terms of reversible physical cross‐links.