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KMID : 1007520210300131685
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Food Science and Biotechnology
2021 Volume.30 No. 13 p.1685 ~ p.1693
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Structure-function relationship of fermented skate skin gelatin-derived bioactive peptides: a peptidomics approach
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Mirzapour-Kouhdasht Armin
Lee Chul-Won
Yun Hyo-Suk
Eun Jong-Bang
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Abstract
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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.
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KEYWORD
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Bioactive peptide, DPP-IV inhibitory activity, ACE inhibitory activity, Peptidomics, Antibacterial peptide, Gelatin
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