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.