Publisert 2023

Les på engelsk


Tidsskrift : ACS Food & Science Technology , vol. 3 , p. 2219–2228–9 , 2023

Utgiver : American Chemical Society (ACS)

Internasjonale standardnummer :
Trykt : 2692-1944
Elektronisk : 2692-1944

Publikasjonstype : Vitenskapelig artikkel

Bidragsytere : Sorokina, Liudmila; Matić, Josipa; Rieder, Anne; Koga, Shiori; Afseth, Nils Kristian; Wilson, Steven Ray Haakon; Wubshet, Sileshi Gizachew



Har du spørsmål om noe vedrørende publikasjonen, kan du kontakte Nofimas bibliotekleder.

Kjetil Aune


Protein hydrolysates from food-processing byproducts are valuable sources of peptides, often diverse in structure and bioactivity. This attribute makes them particularly interesting as health-promoting ingredients with a polypharmacological effect toward complex diseases such as type-2 diabetes. In the present study, dual angiotensin-I-converting enzyme (ACE-1) and dipeptidyl-peptidase 4 (DPP4) inhibitory properties of mechanically deboned chicken residue (MDCR) hydrolysate was investigated. MDCR was hydrolyzed using food-grade protease, and a low-molecular weight (514 Da) peptide fraction was identified with potent dual ACE-1 and DPP4 inhibition. Orthogonal chromatographic fractionation (i.e., size exclusion followed by reversed-phase) coupled with in vitro bioassays resulted in isolation of potent bioactive fractions. Two peptides constituting the potent fractions were identified as IY (IC50 = 7.0 μM for ACE-1) and VL (IC50 = 1.2 mM for DPP4). Low molecular weight peptide fraction from poultry byproduct hydrolysate may serve as a health-promoting functional ingredient with dual blood pressure and blood glucose regulating effect.


Temasider tilknyttet publikasjonen