Kinetics of Thermal Denaturation of β-Lactoglobulin at pH 2.5

Calorimetric Study of Thermal Denaturation of (3-Lactoglobulin

Effects of pH and milk constituents (milk ultrafiltrate and ~:-casein) on denaturation of fl-lactoglobulin were investigated by a dynamic method based on differential scanning calorimetry. The apparent reaction order of /Ltactoglobulin denaturation by the dynamic method was 2.0 over the pH range of 4.0 to 9.0, which is in fair agreement with results by other investigators using more classical m...

Effect of temperature, pH and salt concentration on β-lactoglobulin deposition kinetics studied by OWLS

Thermal aggregation of β-lactoglobulin in presence of metal ions

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Thermal, Chemical and pH Induced Denaturation of a Multimeric β-Galactosidase Reveals Multiple Unfolding Pathways

BACKGROUND In this case study, we analysed the properties of unfolded states and pathways leading to complete denaturation of a multimeric chick pea β-galactosidase (CpGAL), as obtained from treatment with guanidium hydrochloride, urea, elevated temperature and extreme pH. METHODOLOGY/PRINCIPAL FINDINGS CpGAL, a heterodimeric protein with native molecular mass of 85 kDa, belongs to α+β class ...

Kinetics of Thermal Denaturation and Aggregation of Bovine Serum Albumin.

Thermal aggregation of bovine serum albumin (BSA) has been studied using dynamic light scattering, asymmetric flow field-flow fractionation and analytical ultracentrifugation. The studies were carried out at fixed temperatures (60°C, 65°C, 70°C and 80°C) in 0.1 M phosphate buffer, pH 7.0, at BSA concentration of 1 mg/ml. Thermal denaturation of the protein was studied by differential scanning c...