Antioxidant peptides derived from hydrolyzed milk proteins by Lactobacillus strains: A BIOPEP-UWM database-based analysis

Milk protein derived peptides contains YLGYLEQLLR (αS1-casein), VKEAMAPK (β-casein), YIPIQYVLSR (κ-casein) fragment have the promising antioxidant potential by the liquid chromatography-mass spectrometry (LC-MS/MS) coupled with the BIOPEP-UWM database analysis. [Display omitted] •Peptides derived from hydrolyzed milk proteins by L. reuteri WQ-Y1 have the potential antioxidant capacity.•LC-MS/MS coupled with the BIOPEP-UWM database is an outstanding approach for activity peptides detection.•Peptides YLGYLEQLLR (αS1-casein), VKEAMAPK (β-casein), YIPIQYVLSR (κ-casein) fragment had the promising antioxidant potential. Milk-derived peptides have been identified as the essential ingredients in the food industry for the health-promoting properties. Some bioactive peptides in the milk product can be released by the specific protease system of lactic acid bacteria (LAB) during the fermentation processing. In this research, the bioactive peptides released from the casein and whey protein are investigated by the hydrolyzing ability of the Lactobacillus brevis CGMCC15954, Lactobacillus reuteri WQ-Y1 and Lactobacillus plantarum A3. Results found that the hydrolysates of casein/whey protein generated by L. reuteri WQ-Y1 have the potential antioxidant activity. Furthermore, milk-derived peptides identified by the liquid chromatography-mass spectrometry (LC-MS/MS) with the BIOPEP-UWM database showed the YLGYLEQLLR (αS1-casein), VKEAMAPK (β-casein), YIPIQYVLSR (κ-casein) fragment had the promising antioxidant activity, especially VKEAMAPK, which exhibited IC50 of 0.63 and 0.86 mg/mL in DPPH and ABTS free radical scavenging activity. The finding of this study sheds some light of obtaining milk-derived peptides by using the Lactobacillus strains and proves the potential bioactive function of the LAB fermented milk products.