Hydrolysates and peptide fractions from pork and chicken skin collagen as pancreatic lipase inhibitors

The objective of this work was to obtain hydrolysates and peptide fractions from pork (PSC) and chicken (CSC) skin collagen extracts and to evaluate their ability as pancreatic lipase inhibitors. Collagen extracts were hydrolyzed with collagenase or a protease from Bacillus licheniformis (MPRO NX®) at 6, 12, and 24 h. After 24 h incubation, the highest degree of hydrolysis of PSC (p < 0.05) was obtained with collagenase (72.58%), while in CSC was obtained with MPRO NX® (64.45%). Hydrolysates obtained at 24 h had the highest inhibitory activity of lipase (p < 0.05). CSC/collagenase hydrolysates (10 mg/mL) presented the highest inhibitory activity (75.53%) (p < 0.05). Ultrafiltrated fractions >5 kDa from CSC/collagenase and PSC/MPRO NX® hydrolysates were the most bioactive fractions (IC(50): 4.33 mg/mL). The highest were obtained by CSC peptides (IC(50)s: 6.30 and 6.08 mg/mL). These results may be considered as a novel approach to use collagen hydrolysates, or their peptide fractions, as promising natural inhibitors of pancreatic lipase.