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

Abstract

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.

• Authors: Jessica Gathercole, Evelyne Maes, Ancy Thomas, Robert Wieliczko, Anita Grosvenor, Stephen Haines, Stefan Clerens, Santanu Deb-Choudhury
• Journal: Journal of proteomics (J Proteomics) Vol. 273 Pg. 104806 (02 20 2023) ISSN: 1876-7737 [Electronic] Netherlands
• PMID: 36587727 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
• Copyright: Copyright © 2022 Elsevier B.V. All rights reserved.

Chemical References

• Angiotensins
• Dipeptidyl Peptidase 4
• Meat Proteins
• Peptides

Topics

• Humans
• Angiotensins
• Diabetes Mellitus, Type 2
• Digestion
• Dipeptidyl Peptidase 4 (chemistry, metabolism)
• Meat (analysis)
• Meat Proteins
• Peptides (metabolism)