Potential role of the binding of whey proteins to human buccal cells on the perception of astringency in whey protein beverages
Wheyproteinbeverages have been shown to be astringent, which means that they are not appealing to consumers. The exact mechanism of astringency in wheyproteinbeverages is yet to be fully elucidated. In this preliminary study, the binding between ß-lactoglobulin (ß-LG), lactoferrin (LF) and human oral epithelial cells (HSC-2 and NO-1–N-1 cells) at pH 3.5 and pH 7.4 was assayed as a function of protein concentration using an enzyme-linked immunosorbent assay. The binding of ß-LG and LF to HSC-2 and NO-1-N-1 cells was dependent on protein type, protein concentration, pH and time. The intensity of the binding to HSC-2 and NO-1–N-1 cells was much greater for LF than for ß-LG and was protein concentration dependent, which was consistent with the in vivo astringencyperception of LF and ß-LG. The findings demonstrated that the binding interaction between wheyproteins and human oral epithelial cells may play an important role in the perception of astringency in wheyproteinbeverages.