The mesostructure of bovine serum albumin (BSA) at low pH was investigated. Rheological measurements were performed to determine the critical percolation concentration (cp). A decreasing cp with increasing ionic strength was found. Fibrils with a contour length of about 100–300 nm were found using transmission electron microscopy. The measured conversion of monomers into fibrils was independent of ionic strength (0.20–0.30 M). Dilution of BSA samples showed that the aggregation process is reversible and that there exists a critical concentration for the self-assembly of BSA. We explain the decreasing cp with increasing ionic strength in terms of an adjusted random contact model.
|Journal||International Journal of Biological Macromolecules|
|Publication status||Published - 2003|
- heat-induced gelation
- protein gels
Veerman, C., Heck, J., Sagis, L. M. C., & van der Linden, E. (2003). Mesostructure of fibrillar bovine serum albumin gels. International Journal of Biological Macromolecules, 31(4-5), 139-146. https://doi.org/10.1016/S0141-8130(02)00074-0