This work investigated the specific interaction between bovine serum albumin (BSA) and alginate by using multi-spectral measurements and molecular modeling. Alginate did not induce obvious changes of the secondary structure of BSA, but significantly decreased the polarity around tyrosine residues of BSA. The complex between alginate and BSA was formed mainly through hydrogen bonding and electrostatic force. Alginate acted as a stabilizer to increase the stability of BSA during the thermal process. The molecular rearrangement of BSA in the presence of alginate with high charge density led to the formation of a novel and more stable conformational state of alginate-BSA mixture. The rheological analysis indicated that the viscosity of BSA increased with increasing concentrations of alginate. These results revealed some important information about the structure, thermal stability and rheological behavior of hydrocolloid-BSA mixture and provided theoretical guidance for the design of new food hydrocolloids in food industry.
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