Structure-function relationship of fermented skate skin gelatin-derived bioactive peptides: a peptidomics approach

In this study, we investigated the multi-functionality of bioactive peptides derived from fermented skate (Raja kenojei) skin gelatin hydrolysates. The extracted gelatin was hydrolyzed using a combination of food grade subtilisin and actinidin. The hydrolysates were then fractionated via ultrafiltration, and the fractions with the highest dipeptidyl peptidase-IV (DPP-IV) inhibitory, angiotensin-converting enzyme (ACE) inhibitory, and antibacterial proprieties were further purified via ion exchange, solid phase extraction, and reverse phase high performance liquid chromatography. Analysis of the obtained extract revealed a direct relationship between hydrolysis time, degree of hydrolysis, and biological activities. The peptides GRPGNRGE (P1) and AKDYEVDAT (P2), with a molecular weight of 841.42 and 1010.46 Da, respectively, were identified through tandem mass spectrometry. P1 had a lower ACE and DPP-IV inhibitory activity, with a half maximal inhibitory concentration [IC₅₀] of 0.74 and 0.69 mg.mL^-1, respectively, than P2 (0.52 and 0.58 mg.mL^-1, respectively). Antibacterial analysis showed similar results, with a minimum inhibitory concentration of 0.52 and 0.46 mg.mL^-1 against Staphylococcus aureus (highest activity) and 1.75 and 1.44 mg.mL^-1 against Klebsiella pneumonia (lowest activity) for P1 and P2, respectively. Overall, this study revealed two fish gelatin-derived multifunctional peptides, exhibiting ACE inhibitory, DPP-IV inhibitory, and antibacterial activities, as natural nutraceuticals.

The online version contains supplementary material available at 10.1007/s10068-021-00998-6.