title: Fibrillar beta-lactoglobulin gels: Part 3. Dynamic mechanical characterization of solvent-induced systems.
abstract: Oscillatory shear rheometry has been used to study the gelation of beta-lactoglobulin at ambient in 50% v/v trifluoroethanol (TFE)/pH 7 aqueous buffer and in 50% v/v ethanol (EtOH)/water at pH 2. In contrast to what was found on heating aqueous solutions at pH 2 (Part 2 of this series), a more expected "chemical gelation"-like profile was found with modulus components G' and G' ' crossing over as the gels formed and then with G' ' passing through a maximum. In addition, for the EtOH system, there was a significant modulus increase at long time, suggestive of a more complex two-step aggregation scheme. Modulus-concentration relationships were obtained for both systems by extrapolating cure data to infinite time. For the TFE gels, this data was accurately described by classical branching theory, although it could also be approximated by a constant power--law relationship. Only the latter described the modulus--concentration data for the gels in ethanol, but there were problems here of greater frequency dependence of the modulus values and much less certain extrapolation. Gel times for the TFE systems showed higher power laws in the concentration than could be explained by the branching theory in its simplest form being similar, in this respect, to the heat-set systems at pH 2. Such power laws were harder to establish for the EtOH gels as for these there was evidence of gel time divergence close to a critical concentration. Reduced G'/G'inf versus t/tgel data were difficult to interpret for the gels in ethanol, but for the TFE system they were consistent with previous results for the heat-set gels and approximated master curve superposition. The frequency and temperature dependences of the final gel moduli were also studied. In general, the networks induced by alcohols appeared more flexible than those obtained by heating.
authors.affiliation: Department of Life Sciences, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NN, United Kingdom.
authors.forename: Walraj S
authors.initials: WS
authors.lastname: Gosal
authors.forename: Allan H
authors.initials: AH
authors.lastname: Clark
authors.forename: Simon B
authors.initials: SB
authors.lastname: Ross-Murphy
mesh_terms: D000682:Amyloid / Q000737:chemistry; D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry*; D002417:Cattle; D004305:Dose-Response Relationship, Drug; D005782:Gels; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007328:Insulin / Q000737:chemistry; D007477:Ions; D007782:Lactoglobulins / Q000737:chemistry*; D046911:Macromolecular Substances / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D018625:Microscopy, Atomic Force; D008854:Microscopy, Electron; D008894:Milk Proteins / Q000737:chemistry; D009991:Oscillometry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012997:Solvents / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman; D013696:Temperature; D013997:Time Factors; D014867:Water / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: D000682:Amyloid; D001672:Biocompatible Materials; D005782:Gels; D007328:Insulin; D007477:Ions; D007782:Lactoglobulins; D046911:Macromolecular Substances; D008894:Milk Proteins; D012997:Solvents; D014867:Water