title: Theoretical modeling of the kinetics of fibrilar aggregation of bovine beta-lactoglobulin at pH 2.
abstract: The authors propose a kinetic model for the heat-induced fibrilar aggregation of bovine beta-lactoglobulin at pH 2.0. The model involves a nucleation step and a simple addition reaction for the growth of the fibrils, as well as a side reaction leading to the irreversible denaturation and inactivation of a part of the protein molecules. For the early stages of the aggregation reaction, the authors obtain an analytical solution of the model. In agreement with their experimental results, the model predicts a critical protein concentration below where almost no fibrils are formed. The model agrees well with their experimental data from in situ light scattering. By fitting the experimental data with the model, the authors obtain the ionic strength dependent kinetic rate constants for beta-lactoglobulin fibrilar aggregation and the size of the critical nucleus.
authors: Laboratory of Physical Chemistry and Colloid Science, Wageningen University, Dreijenplein 6, 6700 EK Wageningen, The Netherlands. luben.arnaudov@wur.nl
authors: Luben N
authors: LN
authors: Arnaudov
authors: Renko
authors: R
authors: de Vries
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003198:Computer Simulation; D019281:Dimerization; D006863:Hydrogen-Ion Concentration; D007782:Lactoglobulins / Q000737:chemistry* / Q000648:ultrastructure*; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D011485:Protein Binding; D011487:Protein Conformation; D013696:Temperature
chemical_list: D007782:Lactoglobulins; D046912:Multiprotein Complexes