The aim of the present study was to investigate the adsorption
kinetics and the resulting interfacial rheology parameters of tryptic
hydrolysates of b-LG and complexes of protein and different types
of pectin. The interfacial activity and interfacial dilatational characteristics
at the a/w-interface were enhanced for hydrolysed whey
proteins in comparison the unmodified substrate, accordingly this
effect is also expected to be present at the o/w-interface, despite
the different nature of these two interfaces. Furthermore it is
hypothesised, the complexation with pectin further improves the
interfacial rheology parameters, under shear and dilatation,
without a strong reduction in interfacial activity in comparison to
the unmodified substrate and pure protein systems. In this context,
we propose that LMP pectin with a high local charge density may
yield the strongest interfacial complexes due to the high binding
affinity to the proteins. In contrast, HMP and a low local charge
density should result in weaker interfacial layers. Thereby valuable
insights may be gained with respect to the process stability of the
systems under study. A pendant drop tensiometer and an interfacial
shear rheometer were used to characterise pure protein layers
and protein/pectin-complexes with respect to structure formation,
their linear viscoelastic regime and frequency dependence under
both deformation modes.