MAILLARD INDUCED COMPLEXES OF BOVINE SERUM-ALBUMIN - A DILUTE-SOLUTION STUDY

Association of bovine serum albumin (BSA) on heating in the presence a nd absence of 2% xylose has been studied using dynamic light scatterin g and sedimentation velocity. When 3% solutions of the protein alone a re heated at 95 degrees C association products are formed with molar m asses of similar to 2 x 10(6) g/mol, a value which is independent of t he time of heating. These aggregates can be dissociated in solvents th at disrupt non-covalent bonds. When the reducing sugar xylose is prese nt there is a continuous change in the hydrodynamic properties with ti me. After 80 min a molar mass in excess of 7 x 10(6) g/mol is obtained . This increase in molar mass is attributed to additional non-disulphi de linkages resulting from the Maillard reaction. Information about th e gross conformation of the Maillard induced association products has been obtained from MHKS (Mark-Houwink-Kuhn-Sakarada) double logarithmi c plots of D-20,D-w and S-20,S-w against molar mass. The values of the MHKS coefficients obtained are most consistent with a linear rod: i.e . the association is of an end-to-end type.