Maillard induced complexes of bovine serum albumin — a dilute solution study
作者： Azhar Mat Easa , Helen J. Armstrong , John R. Mitchell , Sandra E. Hill , Stephen E. Harding
DOI: 10.1016/0141-8130(96)01090-2
关键词: Bovine serum albumin 、 Reducing sugar 、 Molar mass 、 Sedimentation coefficient 、 Xylose 、 Maillard reaction 、 Dynamic light scattering 、 Chromatography 、 Analytical chemistry 、 Mole 、 Chemistry
摘要: Association of bovine serum albumin (BSA) on heating in the presence and absence 2% xylose has been studied using dynamic light scattering sedimentation velocity. When 3% solutions protein alone are heated at 95 degrees C association products formed with molar masses approximately 2 x 10(6) g/mol, a value which is independent time heating. These aggregates can be dissociated solvents that disrupt non-covalent bonds. reducing sugar present there continuous change hydrodynamic properties time. After 80 min mass excess 7 g/mol obtained. This increase attributed to additional non-disulphide linkages resulting from Maillard reaction. Information about gross conformation induced obtained MHKS (Mark-Houwink-Kuhn-Sakarada) double logarithmic plots D20,w S20,w against mass. The values coefficients most consistent linear rod: i.e. an end-to-end type.
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