The Comparative Heat Stability of Bovine β-Lactoglobulin in Buffer and Complex Media

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

“…At high b-lactoglobulin concentrations, the rate for the aggregation is observed to increase due to the more frequent interactions between protein intermediate species (Roefs and de Kruif, 1994;Hoffmann and van Mil, 1997). Indeed, the kinetics of whey protein, and especially b-lactoglobulin, thermal denaturation has been extensively studied (Lyster, 1970;Sawyer et al, 1971;Hillier and Lyster, 1979;Harwalkar, 1986;Manji and Kakuda, 1987;Dannenberg and Kessler, 1988;Roefs and de Kruif, 1994;Anema and McKenna, 1996;Galani and Apenten, 1997;Chen et al, 1998;Verheul et al, 1998). According to Arnebrant et al (1987) partly denatured proteins are more surface active than native proteins, so it would be expected that a fouling layer forms very rapidly with increased native protein concentration.…”

Solubility and aggregation of commercial α-lactalbumin at neutral pH

“…However, throughout the first 20 min of heating, the t 95 1C values for sample B were much higher than those for sample A. This suggests that hydrophobic interactions were the predominant attractive force at 95 1C, causing the formation of large aggregates, as has been suggested for both a-La (McGuffey et al, 2005) and b-Lg (Galani & Apenten, 1997). The data did not indicate whether hydrophobic interactions led to the formation of disulfide bond or vice versa.…”

A combined theoretical and experimental study to improve the thermal stability of recombinant D‐lactate dehydrogenase immobilized on a novel superparamagnetic Fe3O4NPs@metal–organic framework

“…The Ea was obtained from the slope and A was calculated from the intercept of the Arrhenius plot. After calculation of the Arrhenius constant and the activation energy, the thermodynamic parameters for the variations in entropy (Δ S # ), transition state enthalpy (Δ H # ), and Gibbs free energy (Δ G # ) of heat inactivation were estimated according to the following expressions: where h is Planck's constant (6.6262 × 10 −34 J/s), k B is the Boltzmann constant (1.3806 × 10 −23 J/K) and k is the inactivation rate constant (s −1 ).…”