Cited by 83Protein Hydrolysis and Bioactive PeptidesProteins in Food SystemsFood and Agricultural Sciences

Milk proteins as a source of tryptophan-containing bioactive peptides

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Nongonierma, Alice B., FitzGerald, Richard J.·2015·Food & Function

Abstract

Tryptophan (W) is an essential amino acid which is primarily required for protein synthesis. It also acts as a precursor of key biomolecules for human health (serotonin, melatonin, tryptamine, niacin, nicotinamide adenine dinucleotide (NAD), phosphorylated NAD (NADP), quinolinic acid, kynureric acid, etc.). Among dietary proteins, milk proteins are particularly rich in W. W residues within milk proteins may be released by proteolytic/peptidolytic enzymes either as a free amino acid or as part of peptide sequences. Different W-containing peptides originating from milk proteins have been shown in vitro to display a wide range of bioactivities such as angiotensin converting enzyme (ACE) inhibition along with antioxidant, antidiabetic and satiating related properties. Free W has been shown in certain instances to have an effect on cognition and the aforementioned bioactive properties. However, a higher bioactive potency has generally been observed with specific W-containing peptides compared to free W. Since W is thermolabile, the impact of processing on the stability of W-containing peptides needs to be considered. Milk protein-derived W-containing peptides may have significant potential as natural health promoting agents in humans.

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Registry

Crossref · 10.1039/c5fo00407a

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  • Milk-based proteins can be digested via gastrointestinal peptidases to tryptophan-containing peptides, which in cell and biochemical assays can have biological activities that may positively impact human physiology from blood pressure control to satiation.

    “Milk based proteins in particular can be digested via gastrointestinal peptidases to tryptophan containing peptides, which in cell and biochemical based assays can have biological activities which may positively impact human physiology from blood pressure control to satiation [114].”

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Authors
Nongonierma, A. B., & FitzGerald, R. J.
Affiliations
University of Limerick (IE)
Corresponding author
FitzGerald, Richard J.
Venue
Food & Function
Published
2015
Volume
6
Issue
7
Pages
2115-2127
ISSN
  • 2042-6496 (ISSN-L)
  • 2042-650X
OpenAlex
W2145870957
Cited by
83
References
128
Citations by year
2026: 5 · 2025: 7 · 2024: 7 · 2023: 9 · 2022: 8 · 2021: 10 · 2020: 10 · 2019: 5 · 2018: 6 · 2017: 3 · 2016: 10 · 2015: 3
FWCI
0.71
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • Food & Function (publishedVersion)
  • PubMed (publishedVersion)
  • University of Limerick Institutional Repository (University of Limerick) (acceptedVersion, cc-by-nc-sa)
  • University of Limerick Institutional Repository (University of Limerick) (acceptedVersion, other-oa)
  • Arrow@dit (Dublin Institute of Technology) (submittedVersion, cc-by-nc-sa)
  • Figshare (submittedVersion, cc-by-nc-sa)
  • University of Limerick Institutional Repository (University of Limerick)
Funders
Enterprise Ireland (TC2013-0001)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
Keywords
tryptophan, milk protein, bioactive peptides, tryptophan-containing peptides, free tryptophan, proteolytic enzymes, angiotensin-converting enzyme inhibition, antioxidant activity, antidiabetic activity, satiety, thermolability, food processing, health-promoting peptides, serotonin precursor
MeSH terms
Animals, Humans, Hydrolysis, Milk Proteins, Peptides, Tryptophan

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