In vitro gastrointestinal digestion of highland barley protein: identification and characterization of novel bioactive peptides involved in gut cholecystokinin secretion

Abstract

AbstractBackgroundSatiety hormone cholecystokinin (CCK) plays an important role in food intake inhibition. Its secretion is regulated by dietary components. The search for bioactive compounds that induce CCK secretion is currently an active area of research. The objective of this study was to evaluate the ability of highland barley protein digest (HBPD) to stimulate CCK secretion in vitro and in vivo and identify the responsible peptide sequences.ResultsHBPD was prepared by in vitro gastrointestinal digestion model. The peptides with < 1000 Da in HBPD accounted for 82%. HBPD was rich in essential amino acids Leu, Phe and Val, but lack in sulfur amino acids Met and Cys. HBPD treatment with a concentration of 5 mg/mL significantly stimulated CCK secretion from enteroendocrine STC‐1 cells (P < 0.05). Moreover, oral gavage with HBPD in mice significantly increased plasma CCK level. Chromatographic separation was performed to isolate peptide fractions involved in CCK secretion and peptide sequence was determined by UPLC‐MS/MS. Two novel cholecystokinin‐releasing peptides PDLP and YRIVPL were pointed out for their outstanding CCK secretagogue activity.ConclusionThis study demonstrated for the first time that HBPD had an ability to stimulate CCK secretion in vitro and in vivo and determined the bioactive peptides exerting CCK secretagogue activity in HBPD.This article is protected by copyright. All rights reserved.