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Article Dans Une Revue Journal of Chemical Thermodynamics Année : 2012

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

Résumé

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 preand post-transition base lines gave the most realistic values for Δ�Do(H2O). The value of about 21.6 kJ • mol −1 was obtained for Δ�Do(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. Highlights ► 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.
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Dates et versions

hal-04089379 , version 1 (04-05-2023)

Licence

Paternité - Pas d'utilisation commerciale - Pas de modification

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Mehdi Sahihi, A.K. Bordbar, Y. Ghayeb, N. Fani. Structure-function relationship of β-lactoglobulin in the presence of sodium dodecylbenzenesulfonate. Journal of Chemical Thermodynamics, 2012, 52, pp.16-23. ⟨10.1016/j.jct.2011.12.017⟩. ⟨hal-04089379⟩

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