ArticleJournal of food science2026
Multi-Enzyme Hydrolysis and Ultrafiltration-Based Optimization, Identification, and Characterization of Buttermilk Peptides and Myricetin for Enhancing Antioxidant Synergy.
Article in Journal of food science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Dairy peptides and plant polyphenols attract significant attention for their bioactive properties; however, the synergistic antioxidant mechanism of buttermilk peptides and myricetin remains unclear. In this study, buttermilk proteins from Lacprodan MFGM-10, a milk fat globule membrane (MFGM)-enriched buttermilk powder, were subjected to multi-enzyme hydrolysis using papain (Pap), alkaline protease (AP), and neutral protease (NP) at an enzyme concentration of 6000 U/g in different combinations. The results showed that the synergistic application of enzymes significantly increased the degree of hydrolysis (DH), with the AP group reaching a peak DH of approximately 42% at 150 min. Two candidate peptides, WGSPP and SWPWQ, were selected from the screened buttermilk peptide fractions. Through Caco-2 transmembrane transport validation and molecular docking, it is confirmed that these peptides can non-competitively bind to acetylcholinesterase (AChE) via molecular docking, with binding energies of -12.7 and -11.1 kcal/mol, respectively. Additionally, myricetin exhibits a strong binding energy, with a binding energy of -9.5 kcal/mol. In an L6 myoblast injury model induced by rotenone, combined treatment significantly enhances AChE inhibitory rate, reduces reactive oxygen species (ROS) and malondialdehyde (MDA) levels, restores superoxide dismutase (SOD) activity and the NAD
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