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Impact of wheat gluten on the denaturation of egg white and whey proteins
Author(s) -
Van de Vondel Julie,
Lambrecht Marlies A.,
Delcour Jan A.
Publication year - 2021
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 - 10.1002/cche.10468
Subject(s) - denaturation (fissile materials) , chemistry , egg white , ovalbumin , lysozyme , bovine serum albumin , whey protein , kinetics , biochemistry , biophysics , chromatography , nuclear chemistry , physics , immune system , quantum mechanics , biology , immunology
Background and objectives Wheat gluten (WG) often co‐exists with egg white (EW) and whey proteins in foods. This study investigated the impact of WG on the denaturation of hen egg (S‐)ovalbumin [(S‐)OVA], lysozyme (LYS), and bovine serum albumin (BSA). Findings WG caused the peak temperature of denaturation of LYS and BSA to increase and that of (S‐)OVA to decrease. It accelerated and decelerated denaturation of BSA and OVA, respectively, and their lowered activation energy. In contrast, the denaturation rate of S‐OVA was higher and the activation energy was not affected by the presence of WG. LYS denaturation was reversible, both in the presence and in the absence of WG. Heating induced changes in the surface hydrophobicity of OVA and BSA and changes in the ζ‐potential of LYS, while the levels of their free sulfhydryl groups did not change. Conclusions In model systems, WG impacts both temperatures and kinetics of denaturation of the studied proteins. Hydrophobic interactions between WG and OVA or BSA impact their denaturation kinetics. Significance and novelty This study is the first to demonstrate the impact of WG on the denaturation of EW and whey proteins. These insights will be useful in food product design and further elucidating co‐protein effects.