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:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- FOREIGN
- OSTI ID:
- 1351365
- Journal Information:
- Journal of Agricultural and Food Chemistry, Journal Name: Journal of Agricultural and Food Chemistry Journal Issue: 16 Vol. 63; ISSN 0021-8561
- Publisher:
- American Chemical Society
- Country of Publication:
- United States
- Language:
- ENGLISH
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