Effects of sucrose and sorbitol on the gel formation of a whey protein isolate

Impact of cosolvents (polyols) on globular protein functionality: Ultrasonic velocity, density, surface tension and solubility study

“…For example, the T m value of the b-lg solutions shifted from 75 1C in the absence of cosolvents to 77 1C in the presence of 30 wt% glycerol and 85 1C in the presence of 30 wt% sorbitol. These results are in close agreement with those reported by earlier workers for the influence of glycerol and sorbitol on globular protein thermal stability, e.g., b-lg and BSA (Baier et al, 2004;Baier & McClements, 2003;Chanasattru, Decker, & McClements, 2007a;Dierckx & Huyghebaert, 2002).…”

“…These cosolvents are able to alter the conformation and functional performance of globular proteins in aqueous solutions (McClements, 2002;Saunders, Davis-Searles, Allen, Pielak, & Erie, 2000;Timasheff, 1998Timasheff, , 2002aTimasheff, , 2002b. For example, neutral cosolvents have previously been shown to impact the thermal stability (Baier, Decker, & McClements, 2004;Baier & McClements, 2003;Dierckx & Huyghebaert, 2002), gelation (Baier & McClements, 2001Kulmyrzaev, Bryant & McClements, 2000), foaming (Davis & Foegeding, 2007;Lau & Dickinson, 2005;Murray & Liang, 1999) and emulsion-stabilizing (Kim, Decker & McClements, 2003) performance of globular proteins. The ability of these cosolvents to alter the properties of globular proteins in solution depends on their molecular characteristics, e.g., size, shape and interactions (Timasheff, 1998(Timasheff, , 2002b.…”

Influence of Cosolvent Systems on the Gelation Mechanism of Globular Protein: Thermodynamic, Kinetic, and Structural Aspects of Globular Protein Gelation

“…The stabilizing effect, for example, thermal, cryo-, baro-, and osmo-protective stabilization of mono-and disaccharides is well documented (McClements 2002;Timasheff 2002;Dierckx and Huyghebaert 2002;Semenova and others 2002;others 2000a and2000b;Xie and Timasheff 1997a, 1997cTimasheff 1993;Arakawa and Timasheff 1982). Table 1 gives a brief overview of some of the data available concerning the effect of cosolvent systems on the thermostability of globular proteins.…”

“…A number of polyols, for example, sorbitol, also promote thermostability of globular protein (Dierckx and Huyghebaert 2002;Ashie and others 1999;Athes and Combes 1998;Mozhaev 1996). One of the most important operations in the food industry is thermal processing, for example, pasteurization, sterilization, cooking, freezing, and chilling (Fellows 2000).…”

“…Ikeda (2003) was, however, able to show that in the absence of added NaCl, tan ␦ values were higher at an early stage of gelation, indicative for a more linear aggregation of primary particles, whereas in the presence of salt, self-similar rheological features were exhibited. Rheological studies have shown that carbohydrates and their respective polyols have been shown to affect various stages of the gelation process of globular proteins, by enhancing hydrophobic protein-protein interactions, which have been correlated with an increase in G*, but at the same time the nature of the gel is not affected significantly, because the value of tan ␦ was not altered significantly (Dierckx and Huyghebaert 2002).…”