Probing Conformational Change of Bovine Serum Albumin–Dextran Conjugates under Controlled Dry Heating
The time-dependent conformational change of bovine serum album (BSA) during Maillard reaction with dextran under controlled dry heating has been studied by small-angle X-ray scattering, fluorescence spectroscopy, dynamic light scattering, and circular dichroism analysis. Through the research on the radii of gyration (Rg), intrinsic fluorescence, and secondary structure, conjugates with dextran coating were found to inhibit BSA aggregation and preserve the secondary structure of native BSA against long-time heat treatment during Maillard reaction. The results suggested that the hydrophilic dextran was conjugated to the compact protein surface and enclosed it and more dextran chains were attached to BSA with the increase of the heating time. The study presented here will be beneficial to the understanding of the conformational evolution of BSA molecules during the dry-heating Maillard reaction and to the control of the protein–polysaccharide conjugate structure.
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- FOREIGN
- OSTI ID:
- 1351365
- Journal Information:
- Journal of Agricultural and Food Chemistry, Vol. 63, Issue 16; ISSN 0021-8561
- Publisher:
- American Chemical Society
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
IRRADIATION OF PROTEINS IN THE SOLID STATE. III. INFLUENCE OF OXYGEN AND ABSORBED WATER ON CHANGES PRODUCED IN BOVINE SERUM ALBUMIN
EFFECT OF FATTY ACID ON THE IODINATION OF BOVINE SERUM ALBUMIN