Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7596356 | Food Chemistry | 2014 | 5 Pages |
Abstract
Several bioactive peptides are encrypted within the sequence of major milk proteins, requiring enzymatic proteolysis for release and activation. The present study aimed at the identification of potential anti-inflammatory activities in tryptic hydrolysates of bovine β-casein. Inflammatory processes involve in most cases an activation of Nuclear factor Kappa-light-chain enhancer of activated B cells (NFκB), which is a pro-inflammatory transcription factor of several genes. Hence, a NFκB reporter cell line was established, and TNF-α mediated activation of NFκB was used as a measurement. Bovine β-casein (β-CN) was hydrolysed by trypsin and fractionated by ultrafiltration. Total proteolysate as well as the fraction containing peptides between 1 and 5 kDa showed an inhibitory effect in the cell-based assay, while the fraction containing molecules smaller than 1 kDa did not. This anti-inflammatory effect was ascribed to a group of large, hydrophobic peptides, which were identified using LC-MS. The main peptide was synthesised and showed a significant anti-inflammatory effect in HEKnfkb-RE-cells. Thus, for the first time, a casein-derived peptide having an anti-inflammatory effect in vitro has been identified.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
J. Malinowski, M. Klempt, I. Clawin-Rädecker, P.Chr. Lorenzen, H. Meisel,