Functional improvements in bovine serum albumin-fucoidan conjugate through the Maillard reaction

Abstract

The solubility, thermal stability, surface activity and emulsifying properties of native bovine serum albumin (BSA), heat-treated BSA, a BSA-fiicoidan mixture, and a BSA-fucoidan conjugate were assessed. Covalent linkage of BSA with fucoidan resulted in significantly (p ˂ 0.05) high solubility after heating at 90 degrees C for 15 min, particularly at pH 5. The BSA-fucoidan conjugate had a high melting temperature (97.09 +/- 1.45 degrees C), as found by differential scanning calorimetry, indicating strong heat stability and high resistance to denaturation. Although the attachment of fucoidan, a non-surface-active hydrophilic polysaccharide, gave no change in the surface activity, the emulsifying activity and the emulsion stability of the conjugate at pH 5 were superior to those of native BSA, heat-treated BSA, and the BSA-fucoidan mixture. Conclusively, fucoidan attachment enhanced the solubility, thermal stability and emulsifying properties of the protein molecules with negative charge distribution and steric stabilization. (C) 2015 Elsevier Ltd. All rights reserved.