solutions, and therefore solvent quality for BSA before and after
limited aggregation is almost the same.
On the other hand, it is reasonable to suggest that formation of
the large aggregates of BSATA leads to steric difficulty in their interaction with gelatin, with subsequent collapse of the later. However,In this case it is more probable that formation of the complex particles would result from the simple joining of the BSATA to gelatin without significant changes of the sizes of interacting biopolymers.The relatively higher positive charge of the complex BSATA/gelatin particles as compared with that of the native BSA/gelatin particles also does not promote collapse of the gelatin molecules.
Fig. 9 shows schematically the main structural changes observed
during interaction BSATA with gelatin in coil conformation. BSATA interacts with gelatin molecules resulting in formation large macromolecular associations. The interaction leads to partial
unfolding of the globular protein and to the formation of charged complex particles.