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

Armin Mirzapour-Kouhdasht; Chul Won Lee; Hyosuk Yun; Jong-Bang Eun

doi:10.1007/s10068-021-00998-6

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

Food Sci Biotechnol. 2021 Nov 23;30(13):1685-1693. doi: 10.1007/s10068-021-00998-6. eCollection 2021 Dec.

Authors

Armin Mirzapour-Kouhdasht^{1

2}, Chul Won Lee³, Hyosuk Yun³, Jong-Bang Eun¹

Affiliations

¹ Department of Food Science and Biotechnology, Graduate School of Chonnam National University, 77 Yongbong-ro Buk-gu, Gwangju, 61186 South Korea.
² School of Agriculture and Food Science, University College Dublin, Belfield 4 Dublin, Ireland.
³ Department of Chemistry, Chonnam National University, Gwangju, 61186 South Korea.

Abstract

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.

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

Keywords: ACE inhibitory activity; Antibacterial peptide; Bioactive peptide; DPP-IV inhibitory activity; Gelatin; Peptidomics.