Mesostructure of fibrillar bovine serum albumin gels.
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.
Veerman
Cecile
C
Food Physics Group, Department of Agrotechnology and Food Sciences, Wageningen University, P.O. Box 8129, Bomenweg 2, Wageningen 6700 EV, The Netherlands.
Sagis
Leonard M C
LM
Heck
Jeroen
J
van der Linden
Erik
E
D000818:Animals; D002417:Cattle; D005782:Gels / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D007477:Ions; D008854:Microscopy, Electron; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013696:Temperature; D013997:Time Factors
D005782:Gels; D007477:Ions; D012710:Serum Albumin, Bovine