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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) in the presence of cationic surfactant such as dodecyltrimethyl ammonium bromide (DTAB) have been investigated using various experimental techniques such as UV–vis spectrophotometry, fluorimetry, isothermal titration calorimetry (ITC) and circular dichroism (CD). Subsequently, the retinol binding by β-LG has been investigated in the presence of various amounts of this surfactant as its extrinsic functional binding fluorophore. Comparison of the results allowed to determine the binding of retinol by β-LG in the presence of DTAB. The results of UV–vis and fluorescence studies showed a red shift in wavelength and an increase in absorbance and …