Adsolubilisation of organic compounds onto collagen fibres

Adsolubilisation has been defined as the incorporation to solid–water interfaces of molecules that do not adsorb spontaneously to such interfaces, but can be incorporated through an interaction with an adsorbing surfactant molecule. The aim of this work was to study the adsolubilisation of organic molecules with different hydrophobicity on collagen fibres. Hide powder collagen was treated under mild acidic aqueous conditions with an anionic surfactant, sodium dodecylbenzene sulphonate. Thereafter, five different organic molecules, i.e., benzyl alcohol, 2-naphtol, pararosaniline, hexamethylpararosaniline and nonylphenol with 10 mol ethylene oxide were separately applied to the treated collagen in order to study adsolubilisation as a function of their hydrophobicity.It was found that under acidic conditions all molecules were scarcely adsorbed or not adsorbed by the native hide powder collagen. However, all organic molecules, except benzyl alcohol, were adsolubilised if the hide powder collagen was previously treated with the anionic surfactant. The hydrophobicity of the molecules plays an important role in the adsolubilisation phenomenon with the result that the higher the hydrophobicity (nonylphenol with 10 mol ethylene oxide), the higher the adsolubilisation.

Hydrophobicity plays an important role in the adsolubilisation of organic molecules onto collagen fibres. NP: 2-naphtol, HPRS: hexamethylpararosaniline hydrochloride, NPEO10: nonylphenol with 10 mol ethylene oxide.Figure optionsDownload high-quality image (61 K)Download as PowerPoint slideResearch highlights
► Organic molecules are adsolubilised on collagen fibres modified with an anionic surfactant.
► The hydrophobicity of the molecules plays a major role in the adsolubilisation phenomenon.
► The higher the hydrophobicity of the organic molecules, the higher the adsolubilisation.