| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Institute of Food Research, Norwich Research Park, Colney, Norwich, NR4 7UA, United Kingdom
Correspondence: Address reprint requests to Dr. Steve G. Ring, Institute of Food Research, Norwich Research Park, Colney Lane, Norwich, NR4 7UA, UK. Tel.: +44-(0)1603-255031; Fax: +44-(0)1603-507723; E-mail: steve.ring{at}bbsrc.ac.uk.
The glass-like transition behavior of concentrated aqueous solutions of bovine serum albumin was examined using rheological techniques. At mass fractions >0.4, there was a marked concentration dependence of viscosity with a glass-like kinetic arrest observed at mass fractions in the region of 0.55. At mass fractions >0.6 the material behaved as a solid with a Young's modulus rising from
20 MPa at a mass fraction of 0.621.1 GPa at 0.86. The solid was viscoelastic and exhibited stress relaxation with relaxation times increasing from 33 to 610 s over the same concentration range. The concentration dependence of the osmotic pressure was measured, at intermediate concentrations, using an osmotic stress technique and could be described using a hard sphere model, indicating that the intermolecular interactions were predominantly repulsive. In summary, a major structural relaxation results from the collective motion of the globules at the supra-globule length scale and, at 20°C, this is arrested at water contents of 40% w/w. This appears to be analogous to the glass transition in colloidal hard spheres.
This article has been cited by other articles:
![]() |
R. Parker, T. R. Noel, G. J. Brownsey, K. Laos, and S. G. Ring The Nonequilibrium Phase and Glass Transition Behavior of {beta}-Lactoglobulin Biophys. J., August 1, 2005; 89(2): 1227 - 1236. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |