Characterisation of bovine serum albumin-fucoidan conjugates prepared via the Maillard reaction

Abstract

Bovine serum albumin (BSA)-fucoidan conjugates were prepared by the Maillard reaction (60 degrees C and 79% relative humidity for 96 h), and were then identified by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and size-exclusion chromatography (SEC). Molecular characteristics of the BSA-fucoidan conjugates were investigated, using atomic force microscopy (AFM), dynamic light scattering (DLS), fluorescence spectroscopy, and circular dichroism spectroscopy. SDS-PAGE patterns provided evidence for the covalent bonding between BSA and fucoidan. SEC profiles showed that about 1.5-2.0 tool of fucoidan were covalently linked to 1 mol of BSA, resulting in high-molecular-weight compositions (conjugates). AFM images and DLS results indicated that most particles in the conjugates were nanostructured and more spherical than those of a regular BSA-fucoidan mixture. The fluorescence intensity and maximum emission wavelength of the conjugates together revealed that the BSA molecules had converted from an ordered conformation into a partially folded molten globule state.