Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 1058, Issue -, Pages 228-233Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molstruc.2013.11.009
Keywords
Whey protein; Phenolic acid; Binding mode; Fluorescence spectroscopy; CD; FTIR
Categories
Funding
- China Postdoctoral Science Foundation [2012M520463]
- Beijing Higher Institution Engineering Research Center of Animal Product
- National Science and Technology Support Program Twelfth Five Year Plan [2012BAD12B08]
- China Agricultural University Foreign Experts Project [2012z010]
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Phenolics-rich foods such as fruit juices and coffee are often consumed with milk. In this study, the interactions of alpha-lactalbumin and beta-lactoglobulin with the phenolic acids (chlorogenic acid, caffeic acid, ferulic acid, and coumalic acid) were examined. Fluorescence, CD, and FTIR spectroscopies were used to analyze the binding modes, binding constants, and the effects of complexation on the conformation of whey protein. The results showed that binding constants of each whey protein-phenolic acid interaction ranged from 4 x 10(5) to 7 x 10(6) M-n and the number of binding sites n ranged from 1.28 +/- 0.13 to 1.54 +/- 0.34. Because of these interactions, the conformation of whey protein was altered, with a significant reduction in the amount of a-helix and an increase in the amounts of beta-sheet and turn structures. (C) 2013 Elsevier B.V. All rights reserved.
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