Unlocking the bioactivity of meat proteins: Comparison of meat and meat hydrolysate via simulated gastrointestinal digestion.


Journal

Journal of proteomics
ISSN: 1876-7737
Titre abrégé: J Proteomics
Pays: Netherlands
ID NLM: 101475056

Informations de publication

Date de publication:
20 02 2023
Historique:
received: 20 06 2022
revised: 22 12 2022
accepted: 27 12 2022
pubmed: 2 1 2023
medline: 18 1 2023
entrez: 1 1 2023
Statut: ppublish

Résumé

Understanding the functional attributes of meat proteins is crucial for determining their nutritional benefits. Depending on the form in which meat proteins are available, the digestive process can release peptides which are valuable for nutrition and may also possess bioactive properties, affecting physiology. Liquid chromatography - mass spectrometry (LC-MS) was used to quantitatively compare the molecular peptide features (representing non-redundant peptides), during the different stages of a simulated gastrointestinal digestion process of a minimally processed powdered meat and its enzymatically produced hydrolysate. Results from a principal component analysis (PCA) indicated that the hydrolysate did not undergo extensive additional digestion whereas the powdered meat was digested both at the gastric and in the intestinal phases. Bioactive peptide sequence prediction identified the meat hydrolysate but not the meat powder as the only source of exact and partial bioactive matches in the angiotensin-I converting enzyme and dipeptidyl peptidase IV inhibition categories. Also, a higher source of cryptides (encrypted bioactive peptides), indicated that meat hydrolysates are potentially a better substrate for the release of these enzyme inhibitory peptides. These observations thus suggest that pre-digestion of a complex food matrix such as meat, may enhance its bioavailability following oral consumption early in the digestion process. SIGNIFICANCE: This work highlights enzymatic hydrolysis of meat proteins prior to ingestion allows for potentially higher bioavailability of bioactive peptides that inhibit angiotensin-I converting enzyme and dipeptidyl peptidase IV, thus possibly aiding high blood pressure and type 2 diabetes management.

Identifiants

pubmed: 36587727
pii: S1874-3919(22)00330-X
doi: 10.1016/j.jprot.2022.104806
pii:
doi:

Substances chimiques

Angiotensins 0
Dipeptidyl Peptidase 4 EC 3.4.14.5
Meat Proteins 0
Peptides 0

Types de publication

Comparative Study Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

104806

Informations de copyright

Copyright © 2022 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.

Auteurs

Jessica Gathercole (J)

Smart Foods & Bioproducts, AgResearch Lincoln, New Zealand.

Evelyne Maes (E)

Smart Foods & Bioproducts, AgResearch Lincoln, New Zealand.

Ancy Thomas (A)

Smart Foods & Bioproducts, AgResearch Lincoln, New Zealand.

Robert Wieliczko (R)

Smart Foods & Bioproducts, AgResearch Lincoln, New Zealand.

Anita Grosvenor (A)

Smart Foods & Bioproducts, AgResearch Lincoln, New Zealand.

Stephen Haines (S)

Smart Foods & Bioproducts, AgResearch Lincoln, New Zealand.

Stefan Clerens (S)

Smart Foods & Bioproducts, AgResearch Lincoln, New Zealand; Biomolecular Interaction Centre, University of Canterbury, Christchurch, New Zealand; Riddet Institute, Massey University, Palmerston North, New Zealand.

Santanu Deb-Choudhury (S)

Smart Foods & Bioproducts, AgResearch Lincoln, New Zealand. Electronic address: santanu.deb-choudhury@agresearch.co.nz.

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Classifications MeSH