Effects of structuring and destructuring anionic ions on the rheological properties of thermally induced β-lactoglobulin gels

Influence of moderate electric fields on gelation of whey protein isolate

“…However, the mechanism of protein unfolding and aggregation is complex and may be influenced by many factors, such as electrostatic and hydrophobic interactions, hydrogen bonding and di-sulfide cross-linking (Havea et al, 2002;Kazmierski & Corredig, 2003;Mulvihill, Rector, & Kinsella, 1990). Several studies have shown that the processes of protein unfolding and aggregation occur to different extents depending on the conditions prevailing in the aqueous solution (e.g.…”

Effect of whey protein concentration on the fouling and cleaning of a heat transfer surface

“…At the time a HIWPG is formed, only a fraction of the whey proteins has aggregated (Verheul and Roef, 1998a,b). The magnitude of this fraction, as well as the gel point, depends on many factors such as the gelation pH, temperature and protein concentration (Mulvihill et al, 1990;Langton and Hermansson, 1992;Renard and Lefebvre, 1992;Verheul and Roef, 1998a). HIWPG with high protein concentration tend to form faster due to the increasing rate of aggregation and the decreasing coagulation time (Sharma and Hill, 1993).…”

The dominating effect of ionic strength on the heat-induced denaturation and aggregation of β-lactoglobulin in simulated milk ultrafiltrate

“…Factors influencing the heat-induced denaturation/aggregation of b-lg include non-covalent interactions such as ionic, van der Waals and hydrophobic interactions as well as thiol/ disulphide exchange reactions, leading to the formation of disulphide-linked aggregates (Hoffmann & van Mil, 1997;Mulvihill et al, 1990). Whether these aggregation reactions are irreversible or potentially reversible will depend on the degree of chemical or physical aggregation involved (Verheul et al, 1998) and on factors such as temperature, pH and ionic strength (Hoffmann et al, 1996).…”