Comparative analysis of refolding of chemically denatured β-lactoglobulin types A and B using the dilution additive mode

Thermal stability of β-lactoglobulin in the presence of aqueous solution of alcohols and polyols

“…This result is in good agreement with the data reported by Divsalar [35] and the studies of Apenten and Galani [20,22] who give values of 83.1 and 81.2 • C for ␤-lactoglobulin in 0.05 M glycine-HCl buffer pH 2.6 and concentrations 0.4 and 4 mg ml −1 respectively and differs from values reported by Busti [31] who reports 72.6 ± 0.5 • C at pH 6.8 in phosphate buffer and 88.3 ± 0.2 • C at pH 2.5 citrate buffer. The effect of alcohols and polyols on denaturation temperature depends clearly on the number of OH groups, as well on concentration.…”

Stabilization of Bacillus licheniformis α-amylase by specific antibody which recognizes the N-terminal fragment of the enzyme

“…The Far-UV CD spectra characterize the secondary structure of proteins due to the peptide bond absorption [36]. The Far-UV CD spectra of BLA, TF18K and TF38K fragments are shown in Fig.…”

A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr+3

“…The agreement between the calculated and the experimental results (Fig.1) is striking, and gives considerable support to the use of Eq. 1. , which can be expressed as follows: (5) represents the heat value upon the saturation of all the BLG-A. The apparent association equilibrium constant, K a , as a function of Cr +3 concentration can be calculated as follows: (6) This is remarkable because the intrinsic association equilibrium constants all depend on the properties of the sites on the protein molecule, but the apparent equilibrium constant and the equilibrium composition do not.…”