Indexed on: 16 Aug '16Published on: 16 Aug '16Published in: Journal of Physical Chemistry B
Herein, we report the comparative study of gels and complex coacervates of Bovine Serum Albumin (BSA) and beta-lactoglobulin (β-Lg) and gelatin near to their common pI. Surface patch binding produced variable new soft matter phases (intermolecular complexes) such as opaque coacervates (phase-I, charge neutralized) and transparent gels (phase-II, overcharged complexes). We emphasis the comparative study of the microstructure of coacervates and gels formed at different mixing ratios using small angle scattering (SANS) data. It was found that phase states were entirely dictated by mixing ratio r = [GB]:[β-Lg or BSA]. Thermo-viscoelastic profiles of aforesaid samples revealed lesser storage modulus and lower melting temperature of coacervates compared to gels. Thermally activated samples generated additional states that were probed by SANS and rheology. Thus, it is established that intermolecular association between globular proteins and random coil polypeptide can self-assemble into various soft matter states that may facilitate harvesting of novel biomaterials.