Time of flight mass spectrometry
ULPC-MS/MS
Dipeptide
Tripeptide
Bioactive peptides
Milk protein hydrolysate
TANDEM MASS-SPECTROMETRY
SIMULATED GASTROINTESTINAL DIGESTION
ENZYME-INHIBITORY PEPTIDES
RETENTION TIME PREDICTION
CASEIN-DERIVED PEPTIDES
BIOACTIVE PEPTIDES
CONVERTING-ENZYME
WHEY-PROTEIN
BETA-LACTOGLOBULIN
ASPERGILLUS-NIGER
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 overfragmentation 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 p-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. (C) 2015 Elsevier Ltd. All rights reserved.