Structure–function relationship of β-lactoglobulin in the presence of sodium dodecylbenzenesulfonate

► Stability parameters and retinol binding property of β-lg in the presence of SDBS have been determined at various pH. ► Higher denaturating effect of SDBS at acidic pH can be due to positive charge density of β-lg at this pH. ► SDBS enhances the retinol binding affinity of β-lg in all of its concentration range. ► The β-lg/retinol binding is pH-dependent. Bovine β-lactoglobulin (β-lg) present in milks has been found “in vivo” in complexes with lipids such as butyric and oleic acids. To elucidate the still unknown structure–function relationship in this protein, the structural changes of β-lactoglobulin variant A (β-lg A) were investigated in the presence of sodium dodecylbenzenesulfonate (SDBS) as an anionic surfactant using spectrofluorimetry. Subsequently, the retinol binding was investigated by β-lg in the presence of various amounts of this surfactant as its extrinsic functional binding fluorophore. The comparison of the results allowed for determining the binding of retinol by β-lg in the presence of SDBS. The results of fluorescence studies showed a higher denaturating effect of SDBS at acidic pH that can be due to the positive charge density of β-lg at this pH which was calculated using the Henderson–Hasselbalch equation and pKa values of its ionizable groups. For each transition curve, the conventional method of analysis which assumed a linear concentration dependence of the pre- and post-transition base lines gave the most realistic values for ΔGDo(H2O). The value of about 21.6kJ·mol−1 was obtained for ΔGDo(H2O) at various pH from transition curves. The results of retinol binding studies represented the substantial enhancement of retinol binding affinity of β-lg in the presence of this surfactant at various pH levels. Moreover, the obtained results confirmed that the β-lg/retinol binding was pH-dependent.