Effect of Heat-denatured Bovine Serum Albumin on Complexation and Protection of α-tocopherol,Resveratrol and(-)-epigallocatechin-3-gallate

In this paper,the possibility of heat-denatured BSA (hBSA) binding simultaneously to α-tocopherol,resveratrol and epigallocatechin gallate (EGCG) was demonstrated by competitive experiments,and the protection of hBSA on bioactive components was characterized by structural and antioxidant stability experiments.The results indicated that hBSA bind the three bioactive simultaneously whereas no competition was found between these components. The content of free α-tocopherol,resveratrol and EGCG decreased to 48%,68% and 0% respectively after 48 h storage. On the other hand,the content of α-tocopherol,resveratrol and EGCG after 48 h were 91%,90% and 15% for hBSA-EGCG-α-tocopherol-resveratrol complexes. The reduction in ABTS scavenging capacity of free α-tocopherol,resveratrol and EGCG were 6%,10% and 31% respectively after 288 h,however,13% in the ABTS scavenging capacity of hBSA-EGCG-α-tocopherol-resveratrol complexes was observed. In conclusion,hBSA is a good carrier for loading three active substances simultaneously. The data gathered here can be useful for the development of protein-based encapsulating carriers.