title: Identification of short peptide sequences in complex milk protein hydrolysates.
abstract: Numerous low molecular mass bioactive peptides (BAPs) can be generated during the hydrolysis of bovine milk proteins. Low molecular mass BAP sequences are less likely to be broken down by digestive enzymes and are thus more likely to be active in vivo. However, the identification of short peptides remains a challenge during mass spectrometry (MS) analysis due to issues with the transfer and over-fragmentation of low molecular mass ions. A method is described herein using time-of-flight ESI-MS/MS to effectively fragment and identify short peptides. This includes (a) short synthetic peptides, (b) short peptides within a defined hydrolysate sample, i.e. a prolyl endoproteinase hydrolysate of β-casein and (c) short peptides within a complex hydrolysate, i.e. a Corolase PP digest of sodium caseinate. The methodology may find widespread utilisation in the efficient identification of low molecular mass peptide sequences in food protein hydrolysates.
authors: Department of Life Sciences, University of Limerick, Limerick, Ireland.
authors: Martina B
authors: MB
authors: O'Keeffe
authors: Department of Life Sciences, University of Limerick, Limerick, Ireland. Electronic address: dick.fitzgerald@ul.ie.
authors: Richard J
authors: RJ
authors: FitzGerald
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002853:Chromatography, Liquid; D008894:Milk Proteins / Q000032:analysis*; D010455:Peptides / Q000032:analysis*; D011492:Protein Hydrolysates / Q000032:analysis*; D021241:Spectrometry, Mass, Electrospray Ionization; D053719:Tandem Mass Spectrometry / Q000379:methods
chemical_list: D008894:Milk Proteins; D010455:Peptides; D011492:Protein Hydrolysates
keywords: Bioactive peptides; Dipeptide; Milk protein hydrolysate; Time of flight mass spectrometry; Tripeptide; ULPC–MS/MS