Etude thermodynamique de la dissociation réversible de la β-lactoglobuline B pour des pH supérieurs à 5,5

Association behavior of native ?-lactoglobulin

“…21,33 Between pH 4 and 5.2 the dimers associate and form larger oligomeric structures, possibly octamers, as suggested in literature. 19,21 Note that for ␤-lg B almost the same mass was found at 10 and 20°C (Table I and Figure 2B).…”

“…These observations are consistent with the literature (see Introduction). From the literature values of ␤-lg monomer-dimer 7,10,[12][13][14]18,19,22 association constants below pH 4 and above pH 5.2 and dimer-octamer 6,11,20 association constants between pH 4 and 5.2, we calculated the weight-averaged molecular mass of the protein in a 9 mg mL values from our SANS experiments (9 mg mL Ϫ1 ␤-lg, 0.1M NaCl). The M av values obtained in the present study agree well with the literature values and apart from the statistical and systematic errors, differences may be due to differences in properties between H 2 O and D 2 O.…”

Adsorption Dynamics of α-Lactalbumin and β-Lactoglobulin at Air–Water Interfaces

“…Based on the monomer-dimer equilibrium constant of 5-6 ϫ 10 Ϫ6 mol liter Ϫ1 at pH 7, 20°C (27,28), it can be concluded that ␤-lactoglobulin is a monomer under the conditions employed in this study. The ␣-lactalbumin used in this work is the apo form (it contains less than 0.3 mol Ca ϩϩ per mol of protein).…”

A laboratory investigation of cow and camel whey proteins deposition under different heat treatments

“…5(b)(2)) emanates from the difference of their chemical environment. While at neutral pH, ␤-lg exists as a dimeric form and at 55 • C, it dissociates in a monomeric form, whereas at higher temperatures, ␤-lg is denatured (Georges et al, 1962). At acidic pH, ␤-lg is under octameric form considered as more heat stable than at neutral pH.…”