Low Molecular Weight Peptide Fraction from Poultry Byproduct Hydrolysate Features Dual ACE-1 and DPP4 Inhibition
Liudmila Sorokina, Josipa Matić, Anne Rieder, Shiori Koga, Nils Kristian Afseth, Steven Ray Wilson, Sileshi Gizachew Wubshet
Abstract
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 (IC 50 = 7.0 μM for ACE-1) and VL (IC 50 = 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.