Identification and Characterization of Gastrointestinal-Resistant Angiotensin-Converting Enzyme Inhibitory Peptides from Egg White Proteins

Hongbing Fan, Jiapei Wang, Wang Liao, Xu Jiang, Jianping Wu

Research output: Contribution to journalArticlepeer-review

52 Scopus citations

Abstract

Egg proteins are recognized as excellent sources of bioactive peptides, such as angiotensin-converting enzyme inhibitory (ACEi) peptides. Oral administration of a thermolysin-digested egg white hydrolysate (T-EWH) caused a significant blood pressure reduction in spontaneously hypertensive rats; a further ACEi assay implied that its ACEi activity was enhanced after in vitro gastrointestinal (GI) digestion. These results indicated that T-EWH contained ACEi peptides resisting GI digestion?and/or being further released during GI digestion. Therefore, the objective of this study was to identify these responsible?ACEi peptides from T-EWH. The conventionally activity-guided fractionation was applied, coupled with a synchronized GI digestion throughout, during which both peptide yield and ACEi activity before and after the GI digestion were measured. Finally, six ACEi peptides (LAPYK, LKISQ, LKYAT, INKVVR, LFLIKH, and LGHWVY) with good GI resistance were identified with IC50 values <20 μM, especially LKYAT (0.09 μM). The structure?activity relationship of these peptides was discussed. The discovery of GI-resistant ACEi peptides could further support the application of egg white proteins as functional food ingredients.

Original languageEnglish
Pages (from-to)7147-7156
Number of pages10
JournalJournal of Agricultural and Food Chemistry
Volume67
Issue number25
DOIs
StatePublished - Jun 26 2019

Bibliographical note

Publisher Copyright:
Copyright © 2019 American Chemical Society.

Keywords

  • ACE inhibitory peptides
  • egg white
  • gastrointestinal digestion
  • purification and identification
  • structure-activity relationship

ASJC Scopus subject areas

  • General Chemistry
  • General Agricultural and Biological Sciences

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