Self-healing fish gelatin/sodium montmorillonite biohybrid coacervates: structural and rheological characterization.
Complex coacervation driven by associative electrostatic interactions was studied in mixtures of exfoliated sodium-montmorillonite (Na(+)-MMT) nanoplatelets and fish gelatin, at a specific mixing ratio and room temperature. Structural and viscoelastic properties of the coacervate phase were investigated as a function of pH by means of different complementary techniques. Independent of the technique used, the results consistently showed that there is an optimum pH value at which the coacervate phase shows the tightest structure with highest elasticity. The solid-like coacervates showed an obvious shear-thinning behavior and network fracture but immediately recovered back into their original elastic character upon removal of the shear strain. The nonlinear mechanical response characterized by single step stress relaxation experiments revealed the same trend for the yield stress and isochronal shear modulus of the coacervates as a function of pH with a maximum at pH 3.0 and lower values at 2.5 and 3.5 pHs, followed by a very sharp drop at pH 4.0. Finally, small-angle X-ray scattering (SAXS) data confirmed that at pHs lower than 4.0 the coacervate phases were dense and structured with a characteristic length scale (ξ(SAXS)) of ~7-9 nm. Comparing the ξ(SAXS) with rheological characteristic length (ξ(rheol)) estimated from low-frequency linear viscoelastic data and network theory, it was concluded that both the strength of the electrostatic interactions and the conformation of the gelatin chains before and during of the coacervation process are responsible for the structure and rigidity of the coacervates.
Polymer Division, School of Chemistry, College of Science, University of Tehran, Tehran, Iran. ntaheri@khayam.ut.ac.ir
Nader Taheri
NT
Qazvini
Sreenath
S
Bolisetty
Jozef
J
Adamcik
Raffaele
R
Mezzenga
D001546:Bentonite / Q000737:chemistry*; D003102:Colloids; D004548:Elasticity; D029941:Fish Proteins / Q000737:chemistry*; D005780:Gelatin / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008027:Light; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry*; D011487:Protein Conformation; D012212:Rheology; D053838:Scattering, Small Angle; D014783:Viscosity; D014961:X-Ray Diffraction
D003102:Colloids; D029941:Fish Proteins; D001546:Bentonite; D005780:Gelatin