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Gosal, Walraj S, Clark, Allan H 
ORCID: https://orcid.org/0000-0003-2965-8941 and Ross-Murphy, Simon B
(2004)
Fibrillar beta-lactoglobulin gels:Part 2. Dynamic mechanical characterization of heat-set systems.
Biomacromolecules, 5 (6).
pp. 2420-9.
ISSN 1525-7797
Abstract
Oscillatory shear rheometry (mechanical spectroscopy) has been used to study the heat-set gelation of beta-lactoglobulin at pH 2. Modulus-concentration relationships were obtained by extrapolating cure data to infinite time. In terms of theory, these fail to provide a clear distinction between the fractal description of biopolymer gels and the classical random f-functional polycondensation branching theory (cascade) approach, though the latter is preferred. Critical exponents for the sol-gel transition, derived from these data, are also discussed. Where gel time-concentration results are concerned the fractal model makes no predictions, and the cascade approach in its simplest form must be rejected in favor of a more sophisticated version involving delivery of fibrils by nucleation and growth into the random aggregation process. Over the limited concentration range accessed experimentally, cure data for the different beta-lactoglobulin solutions, reduced to the universal form G'/G'inf versus t/tgel, superimposed well for samples heated both at 80 and 75 degrees C and for different batches of protein. Studies of the frequency responses of the fully cured gels confirm the validity of the gel description given to these materials, and a study of the temperature dependence of the frequency spectrum suggests a fall in the elastic component of the modulus as temperature decreases. This contrasts with what has been found for other heat-set globular protein gels such as those from serum albumin where the gel modulus increases at lower temperatures. The present results are in good agreement with more limited amounts of pH 2 beta-lactoglobulin data published earlier, though some differences arise through a previous neglect of measurement "dead time".
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | amyloid,animals,biocompatible materials,cattle,dose-response relationship, drug,gels,hot temperature,hydrogen-ion concentration,insulin,ions,lactoglobulins,macromolecular substances,magnetic resonance spectroscopy,microscopy, atomic force,microscopy, electron,milk,oscillometry,protein conformation,protein structure, secondary,solvents,spectroscopy, fourier transform infrared,spectrum analysis, raman,temperature,thermodynamics,time factors,water,x-ray diffraction |
| Faculty \ School: | Faculty of Medicine and Health Sciences > Norwich Medical School |
| UEA Research Groups: | Faculty of Medicine and Health Sciences > Research Groups > Epidemiology and Public Health Faculty of Medicine and Health Sciences > Research Groups > Health Services and Primary Care Faculty of Medicine and Health Sciences > Research Groups > Norwich Clinical Trials Unit Faculty of Medicine and Health Sciences > Research Groups > Public Health and Health Services Research (former - to 2023) Faculty of Medicine and Health Sciences > Research Centres > Population Health |
| Depositing User: | Pure Connector |
| Date Deposited: | 27 Jan 2014 13:26 |
| Last Modified: | 19 Oct 2023 01:13 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/46110 |
| DOI: | 10.1021/bm049660c |
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