Effect of surfactant addition on particle properties of whey proteins and their subsequent complexation with salivary proteins
Madadlou, Ashkan | Zamani, Somayeh | Lu, Yixing | Abbaspourrad, Alireza | Science et Technologie du Lait et de l'Oeuf (STLO) ; Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST | Department of Food Science, College of Agriculture & Life Sciences ; Cornell University [New York]
The astringency of acidified whey protein beverages is unpleasant to consumers and a challenge to theindustry to overcome. It may be associated with whey-salivary protein interactions. We examined theinfluence of complexation of whey proteins with a low molecular weight surfactant (Tween) on somecharacteristics of subsequently formed whey-salivary protein aggregates. Surface tension measurementsindicated that hydrophobic interaction between Tween and whey proteins was initiated at a Tween-to-WPI ratio of 1:50. Tween dissociated b-lactoglobulin dimers to monomers, decreased the size and percentageof non-soluble aggregates (>4000 nm) and decreased the z-potential of WPI samples. Surfactantcomplexation also decreased the surface hydrophobicity of whey proteins. In addition, based on Fouriertransforminfrared spectroscopy, surfactant reduced intermolecular protein interactions. Nonetheless,measurement of accessible thiol group content revealed that surfactant-whey protein interaction did notunfold the proteins. Surfactant complexation resulted in smaller aggregates and a lower turbidity ofwhey protein-saliva mixture.
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