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Updated: Sep 27, 2026

Controlled Strain of 3D Hydrogels under Live Microscopy Imaging
Published on: December 4, 2020
Mesostructure of fibrillar bovine serum albumin gels
Cecile Veerman1, Leonard M C Sagis, Jeroen Heck
1Food Physics Group, Department of Agrotechnology and Food Sciences, Wageningen University, P.O. Box 8129, Bomenweg 2, Wageningen 6700 EV, The Netherlands.
Abstract:
The mesostructure of bovine serum albumin (BSA) at low pH was investigated. Rheological measurements were performed to determine the critical percolation concentration (c(p)). A decreasing c(p) 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 c(p) with increasing ionic strength in terms of an adjusted random contact model.
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