The
technique of in situ particle film attenuated total reflection
Fourier transform infrared spectroscopy (ATR FTIR) has been used to
probe the adsorption and coadsorption (sequential) of a common food
protein (β-lactoglobulin, BLG) and two representative bile salts
(taurocholic acid and glycocholic acid, abbreviated as TCA and GCA)
onto the surface of titanium dioxide (TiO2) nanoparticles.
Evaluating of binding interactions between commonly used (historically
now, in some countries) food additives and food components, as well
as the body’s own digestion chemicals, is a critical step in
understanding the role of colloidal phenomena in digestion and bioavailability.
TCA is found to adsorb onto TiO2 but without any significant
ability to be retained when it is not present in the aqueous phase.
GCA is also found to adsorb via two distinct binding mechanisms, with
one type of adsorbed species being resistant to removal. BLG adsorbs,
is irreversibly bound, and has altered conformation when adsorbed
at pH 2 (stomach conditions) to the conformation when adsorbed at
pH 6.5 (small intestine conditions). This altered conformation is
not interface-dependent and is mirrored in the solution spectra of
BLG. Sequential coadsorption studies indicate that TCA and GCA adsorb
onto TiO2 nanoparticle surfaces and display similar degrees
of reversibility and binding in the presence or absence of preadsorbed
BLG.