Interfacial and foaming properties of sulfydryl-modified bovine β-lactoglobulin

Atmospheric pressure cold plasma (ACP) treatment of whey protein isolate model solution

“…This behaviour could be explained by the formation of aggregates among proteins, as confirmed by the free SH group analysis, size distribution test and HPLC profiles, that seems to play a negative role in the foam formation. The foam behaviour has been intensively studied by different Authors under different processing conditions and for some extend it is not enough clear (Kinsella, 1981;Zhu and Damodaran, 1994;Nicorescu et al, 2009;Horozov, 2008;Croguennec, Renault, Bouhallab, & Pezennec, 2006;Bouaouina, Desrumaux, Loisel, & Legrand, 2006;Uzun, Ibanoglu, Catal, & Ibanoglu, 2012). Many parameters are involved in the capacity to foam formations and in this study the first hand information obtained suggested that a relatively short time treatment was able to improve the functionality of the model system.…”

Interfacial properties of heat-treated ovalbumin

“…Results we obtained with native and non-native monomers of β-lactoglobulin supported this observation. In fact, native β-lactoglobulin developing film with higher viscoelasticity on aging than non-native monomers of β-lactoglobulin has a lower ability to stabilize foams [41]. Kinetics of both protein adsorption and proteins unfolding at the interface for developing interactions with neighboring molecules appeared to be highly relevant for the mechanism of foam stabilization.…”

Rheological properties of protein films

“…One might expect disulfide bond exchange to play a large role in the formation of stronger films on heating, though in fact Renault et al [69] have shown that an increase in G i for ovalbumin films may be more strongly linked to an increase in intermolecular β-sheets. The same research group has also produced clear evidence [70] that sulfhydryl blocked ovalbumin can form even stronger films and form more stable foams. This has strengthened arguments [71 •• ] that the high interfacial shear rheology of protein films may be more due to physical close packing of protein molecules with net-repulsive interactions, rather than specific strong cross-links between the adsorbed molecules.…”