[en] Enzymatic hydrolysis of wheat gluten protein improves its solubility and produces hydrolysates withfoaming properties which may find applications in food products. First, we here investigated whetherfoam-liquid fractionation can concentrate wheat gluten peptides with foaming properties. Foam andliquid fractions had high and very low foam stability (FS), respectively. In addition, foam fractions wereable to decrease surface tension more pronouncedly than un-fractionated samples and liquid fractions,suggesting they are able to arrange themselves more efficiently at an interface. As a second objective,foam fractionation served as a tool to study the structural properties of the peptides, causing thesedifferences in air-water interfacial behavior. Zeta potential and surface hydrophobicity measurements didnot fully explain these differences but suggested that hydrophobic interactions at the air-water interfaceare more important than electrostatic interactions. RP-HPLC showed a large overlap between foam andliquid fractions. However, a small fraction of very hydrophobic peptides with relatively high averagemolecular mass was clearly enriched in the foam fraction. These peptides were also more concentratedin un-fractionated DH 2 hydrolysates, which had high FS, than in DH 6 hydrolysates, which had low FS.These peptides most likely play a key role in stabilizing the air-water interface.
Disciplines :
Food science
Author, co-author :
Wouters, Arno G.B.
Rombouts, Ine
Schoebrechts, Nele
Fierens, Ellen
Brijs, Kristof
Blecker, Christophe ; Université de Liège > Agronomie, Bio-ingénierie et Chimie (AgroBioChem) > Science des alim. et formul.
Delcour, Jan A.
Language :
English
Title :
Foam fractionation as a tool to study the air-water interfacestructure-function relationship of wheat gluten hydrolysates
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