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

Milk-derived peptides have been identified as the essential ingredients in the food industry for the healthpromoting 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, milkderived peptides identified by the liquid chromatography-mass spectrometry (LC-MS/MS) with the BIOPEPUWM database showed the YLGYLEQLLR (alpha S1-casein), VKEAMAPK (beta-casein), YIPIQYVLSR (kappa-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.

Automated summary

This research investigated the bioactive peptides released from casein and whey protein by Lactobacillus strains. The hydrolysates generated by Lactobacillus reuteri WQ-Y1 showed potential antioxidant activity, and specific milk-derived peptides were identified with promising antioxidant properties. These findings demonstrate the potential bioactive function of LAB fermented milk products.