Food-Derived Bioactive Peptides Influence Gut Function

Abstract

Bioactive peptides either present in foods or released from food proteins during digestion have a wide range of physiological effects, including on gut function. Many of the bioactive peptides characterized to date that influence gut motility, secretion, and absorption are opioid agonists or antagonists. The authors review a body of experimental evidence that demonstrates an effect of peptides from food proteins on endogenous (nondietary) protein flow at the terminal ileum of simple-stomached mammals, including adult humans. At least some dietary peptides (1000-5000 Da) significantly enhance the loss of protein from the small intestine, causing an increased amount of protein to enter the colon. Food-derived peptides appear to either stimulate protein secretion into the gut lumen or inhibit amino acid reabsorption or influence both processes simultaneously. The effect of dietary peptides on small-intestine secretory-protein dynamics is discussed in the context of the major components of gut endogenous protein, sloughed cells, enzymatic secretions, mucin, and bacterial protein.

The effect of carbohydrate and marine peptide hydrolysate co-ingestion on endurance exercise metabolism and performance

“…Subsequently, exogenous CHO oxidation may have been reduced as a consequence of the delayed absorption of co-ingested CHO within the CHO-PRO condition [26,27], in which greater reliance would have been placed upon endogenous CHO reserves. In contrast, it is also possible that the inclusion of peptides within the CHO-PRO-PEP condition may have enhanced gastric emptying and gastrointestinal uptake of CHO via the up-regulation of additional intestinal co-transporters [17,28-30]. Again, however, further measurements of gut motility and absorption kinetics are required to verify the influence of solution osmolality.…”

Dietary Protein Structure Affects Endogenous Ileal Amino Acids But Not True Ileal Amino Acid Digestibility in Growing Male Rats

“…However, for convenience, a casein hydrolysate, prepared from an enzymatic digest of intact casein, is used as a model protein hydrolysate, and it is assumed that the basal EIAA flows determined based on alimentation with the casein hydrolysate are similar to basal EIAA flows determined after alimentation with hydrolysates derived from protein sources (not containing fiber or ANFs) other than casein. The latter assumption may be challenged because it is possible that there are bioactive peptides present in the casein hydrolysate that may lead to increased or decreased secretion of endogenous proteins into the gastrointestinal tract and that any bioactive peptides present may differ for different hydrolysates (40).…”

Mass spectrometry for nutritional peptidomics: How to analyze food bioactives and their health effects

“…Finally, many peptides do exhibit opioid activity either in agonist or antagonist mode. For a detailed review on bioactive peptides and their influence on gut function, readers are referred to the review from Moughan and colleagues [101]. In relation to milk, this has particular importance in delivering bioactive proteins and peptides to infants whose mucosal barrier in the gastrointestinal tract is delayed in maturation.…”