| Summary: | ABSTRACT: Milk protein concentrate was hydrolyzed using one-step enzymatic hydrolysis. Both the peptide profiles and antioxidant activities of the resulting extensive hydrolysates of milk protein concentrate (EMPH) were analyzed using a peptidomics approach based on liquid chromatography–tandem mass spectrometry. The results demonstrated that the degrees of hydrolysis of the 4 EMPH by Alcalase-Protamex, Alcalase-Protease A 2SD, Alcalase-Flavorzyme, and Alcalase-ProteAXH were 12.02%, 16.85%, 15.87%, and 15.77%, respectively. Using size exclusion chromatography, 99.85% of the peptides in the Alcalase-Protease A 2SD hydrolysate were shown to have a molecular weight of <3 kDa. A total of 33 common peptides were identified in the EMPH by liquid chromatography–tandem mass spectrometry, 16 of which were identified as bioactive peptides using bioinformatics. The peptide profiles and the coverage of master proteins of the 4 EMPH were different. The EMPH also exhibited strong free radical scavenging capacity, as indicated by the results of the 1,1-diphenyl-2-picrylhydrazyl radical, 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid), hydroxyl radical, and reducing power assays. The results of this study provided useful information on the peptide profiles and antioxidant activity of EMPH.
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