Purpose. To characterize via electron spectroscopy for chemical analysis (E
SCA) the surface of spray-dried particles of trehalose plus a protein (bovi
ne serum albumin). Additionally, to show how and why the addition of a surf
actant reduces protein adsorption, and by this mechanism could reduce prote
in instability during spray-drying.
Methods. Aqueous solutions of trehalose plus bovine serum albumin (bSA) wer
e spray-dried with increasing concentrations of surfactant. The surface com
position of the dried particles was examined using ESCA.
Results. The presence of bSA, trehalose, and surfactant could be detected q
uantitatively in the particle surface. In the absence of surfactant the bSA
had a large surface excess concentration (determined via its N atoms). Inc
reasing concentration of polysorbate 80 reduced the surface excess of bSA i
n a concentration-dependent manner. At high polysorbate 80 concentration (5
mg/ml) the bSA could no longer be detected in solid surface. Using sodium
dodecyl sulfate it was shown that the reduction in surface concentration of
the protein is accompanied by a simultaneous increase in surface concentra
tion of the surfactant. Neither surfactant fully covers the surface at the
point of complete protein exclusion.
Conclusions. ESCA provides a direct, quantitative measure of the surface co
mposition of spray-dried trehalose/protein/surfactant particles. Surfactant
reduces protein adsorption at the water/air-interface. This appears to be
a result of complex formation with the surfactant within the bulk spray sol
ution.