α-Lactalbumin (α-La) and glycomacropeptide (GMP) were separated using heparin affinity chromatography and a one step elution with 1 M NaCl. The eluted peaks were separated by RP-HPLC and identified by N-terminal sequencing followed by matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometry. This study showed that proteolytic activity in whey results in cleavage of at least 12 sites in the 23 N-terminal amino acids of αs1-casein (CN). The greatest concentrations of the 1-23 N-terminal amino acids were found in the α-La product, whereas the greatest concentration of the 1-9 (heparin binding motif) and 1-13 fragments were found in GMP and whey protein concentrate (WPC). The finding of an intact heparin binding 1-23 peptide in the α-La product may account for some of its reported activity against enteropathogenic E. coli.
|Original language||English (US)|
|Number of pages||4|
|State||Published - 2001|
ASJC Scopus subject areas
- Food Science