Protein digestomic analysis reveals the bioactivity of deer antler velvet in simulated gastrointestinal digestion

Food Res Int. 2017 Jun:96:182-190. doi: 10.1016/j.foodres.2017.04.002. Epub 2017 Apr 5.

Abstract

Proteins are the most prominent bioactive component in deer antler velvet. The aim of the present study was to track the fate of protein of antler velvet by protein digestomics. The peptide profile identified by LC-MS/MS and the in vitro bioactivity of antler velvet aqueous extract (AAE) were investigated in simulated gastrointestinal digestion. A total of 23, 387 and 417 peptides in AAE, gastric and pancreatic digests were identified using LC-MS/MS, respectively. Collagens, the predominant proteins, released 34 peptides in gastric digests and 146 peptides in pancreatic digests. The gastric and pancreatic digests presented dipeptidyl peptidase IV (DPP-IV) and prolyl endopeptidase (PEP) inhibition activities. Four peptides from digests were proved to be DPP-IV and PEP inhibitory peptides. The results showed that the peptides released from antler velvet protein contributed to the bioactivity of antler velvet during digestion.

Keywords: 2-Mercaptoethanol (PubChem CID: 1567); Antler velvet; Bioactivity; Diprotin A (PubChem CID: 3107); Gly-Pro-p-nitroanilide hydrochloride (PubChem CID: 16219380); In-vitro digestion; LC-MS/MS; Peptides; Protein digestomics; Z-Gly-Pro-p-nitroanilide (PubChem CID: 16218813); o-Phthalaldehyde (PubChem CID: 4807).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antlers / metabolism*
  • Chromatography, Liquid
  • Deer*
  • Digestion*
  • Dipeptidyl-Peptidase IV Inhibitors / metabolism
  • Dipeptidyl-Peptidase IV Inhibitors / pharmacology
  • Gastric Juice / chemistry
  • Hydrolysis
  • Intestinal Secretions / chemistry
  • Male
  • Peptide Fragments / metabolism*
  • Peptide Fragments / pharmacology
  • Prolyl Oligopeptidases
  • Proteins / metabolism*
  • Proteins / pharmacology
  • Proteolysis
  • Proteomics / methods
  • Serine Endopeptidases / drug effects
  • Serine Endopeptidases / metabolism
  • Serine Proteinase Inhibitors / metabolism
  • Serine Proteinase Inhibitors / pharmacology
  • Tandem Mass Spectrometry

Substances

  • Dipeptidyl-Peptidase IV Inhibitors
  • Peptide Fragments
  • Proteins
  • Serine Proteinase Inhibitors
  • Serine Endopeptidases
  • Prolyl Oligopeptidases