Nagai, Takeshi
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Characterization of Fish Skin Hydrolysates Exhibiting Dipeptidyl Peptidase IV Inhibitory Activity Miyamoto, Honoka; Safitri, Erwina; Nagai, Takeshi; Saito, Masataka
Indonesian Food and Nutrition Progress Vol 21, No 1 (2024)
Publisher : Indonesian Association of Food Technologists

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22146/ifnp.88534

Abstract

Dipeptidyl peptidase IV (DPP-IV) inhibitors are antidiabetic drugs that can lower blood sugar levels. There are still few reports on the DPP-IV inhibitory activity of peptides obtained from discarded fish skin. Therefore, we prepared various enzymatic hydrolysates using the skins of six fish species and investigated their DPP-IV inhibitory effects. As a result, it was found that the DPP-IV inhibitory activity of yellowtail hydrolysate by Alcalase was higher than that of other enzymes. In addition, the IC50 after ethanol fractionation was found to be lower in yellowtail and eel skin hydrolysate. Amino acid composition analysis showed that the hydrolysate obtained from the skin of the yellowtail contained the highest amount of Gly, followed by Pro, Hyp, and Ala, indicating that it was a peptide derived from type I collagen. Fractionation with ethanol showed that the DPP-IV inhibitory components were contained in the low molecular weight fraction. The artificial digestion test observed no DPP-IV inhibitory activity or average molecular weight change. The DPP-IV inhibitory peptide obtained from fish skin has the potential to be applied as a food material to various food products.
Food Functionality Evaluation of Enzymatic Hydrolysates Prepared from Edible Sea Cucumber Body Walls Safitri, Erwina; Owada, Mayu; H. Kuziel, Olivia; Mizuta, Shoshi; Nagai, Takeshi; Saito, Masataka
Indonesian Food Science and Technology Journal Vol. 9 No. 2 (2026): Volume 9 Number 2, July 2026 |IFSTJ|
Publisher : Department of Technology of Agricultural product (THP) Jambi University

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.22437/ifstj.v9i2.52617

Abstract

Bioactive peptides from marine organisms, particularly sea cucumbers, represent a promising source of functional compounds with potential health benefits. This study investigated the bioactivities of hydrolysates prepared from several sea cucumber species using five proteolytic enzymes: Alcalase, bromelain, trypsin, papain, and pepsin. The hydrolysates were analyzed for angiotensin-converting enzyme (ACE) inhibitory activity, dipeptidyl peptidase-IV (DPP-IV) inhibitory activity, antioxidant capacity, and molecular weight distribution. Among the samples, 24-h Alcalase hydrolysates of red giant and Kinko sea cucumbers exhibited the highest combined ACE and DPP-IV inhibitory activities. Antioxidant analysis revealed that low DPPH radical scavenging activity showed relatively high oxygen radical absorbance capacity (ORAC) values, indicating different mechanisms of antioxidant action. Ethanol fractionation effectively enhanced ACE and DPP-IV inhibition as well as antioxidant activity. Amino acid composition analysis indicated proteins consistent with type I collagen as the primary source. Enzyme kinetics showed competitive inhibition for ACE and mixed-type inhibition for DPP-IV. Simulated gastrointestinal digestion caused only minor reductions in activity, suggesting that sea cucumber-derived peptides retain their bioactivity under physiological conditions. These findings highlight the potential of sea cucumber hydrolysates as nutraceutical ingredients.