Interactions between Vaccinium bracteatum Thunb. Leaf Pigment and Rice Protein
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Abstract:
Combined proteomic and biochemical strategies were used to study the interaction between Vaccinium bracteatum Thunb. Leaf (VBTL) pigment and rice protein. Changes in antioxidant activity and free polyphenol content of VBTL pigment were measured before and/or after the dyeing process. Changes in surface hydrophobicity and secondary structure of the protein were also analyzed. The results indicated that the antioxidant activity and free polyphenol content of VBTL pigment decreased by 67.19% and 68.11%, respectively, after dyeing the rice protein. Meanwhile, the brightness and surface hydrophobicity of rice protein decreased significantly. In addition, the dyeing process changed secondary structure of rice protein.. Briefly, there were significant reductions in the content of α-helix and β-sheet structures, but an obvious increase in random coil. Furthermore, the results indicated that albumin interacted more readily with VBTL pigment than did globulin or glutelin. All the data indicated that the VBTL pigment interacted with rice protein mainly via hydrophobic bonds and hydrogen bonds.
