Bovine Milk Protein-Derived Preparations and Their Hydrolysates as Sources of ACE-Inhibitory, DPP-IV-Inhibitory, and Antioxidative Peptides Analyzed Using in Silico and in Vitro Protocols

Abstract

Bovine milk protein preparations (MPPs), namely micellar casein concentrate (MCC), serum protein concentrate (SPC), and MCC with ultrafiltrated buttermilk permeate (MBP), were analyzed as sources of inhibitors of angiotensin-converting enzyme (i.e., ACE) and dipeptidylpeptidase IV (i.e., DPP-IV) as well as antioxidative peptides. The studies involved in silico predictions of the release of biopeptides from bovine milk proteins. Then, all MPPs were subjected to the simulated gastrointestinal digestion using the INFOGEST protocol. Results using a BIOPEP-UWM database tool indicated that 59 biopeptides exhibiting the above-mentioned activities could be produced upon the action of pepsin, trypsin, and chymotrypsin. Thirty-six biopeptides were identified in at least one of the three MPPs subjected to the INFOGEST protocol. MCC before simulated digestion exhibited the strongest ACE-inhibiting activity among all MPPs (IC50 = 1.856 mg/mL). The weakest ACE inhibitory effect was demonstrated for MBP after duodenal digestion (i.e., MBP D; IC50 = 7.627 mg/mL). The above MPP showed the strongest DPP-IV-inhibiting activity (IC50 = 0.0067 mg/mL). All MPPs exhibited antioxidative activity, with the strongest ABTS•+ (i.e., 2,2′-azino-bis(3-ethylbenzotialozline-6-sulfonic acid) radical scavenging effect shown for MBP D (IC50 = 2.754 mg/mL), and the strongest DPPH• (i.e., 2,2-diphenyl-β-picrylhydrazyl) radical scavenging activity (IC50 = 1.238 mg/mL) demonstrated for SPC D. Among all MPPs, SPC D also exhibited the highest FRAP (i.e., Ferric Reducing Antioxidant Power) bioactivity (IC50 = 13.720 mg/mL), whereas MBP D was the MPP with the lowest FRAP potential (IC50 = 20.140 mg/mL). The present study results show the potential of all MPPs as functional additives to support health-beneficial functions of dairy products.

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