{"title":"In silico and in vitro assessment of yellowfin tuna skin (Thunnus albacares) hydrolysate antioxidation effect","authors":"Dian Wahyu Wardani , Andriati Ningrum , Manikharda , Nurul Vanidia , Heli Siti Helimatul Munawaroh , Eko Susanto , Pau-Loke Show","doi":"10.1016/j.fhfh.2023.100126","DOIUrl":null,"url":null,"abstract":"<div><p>The protein hydrolysate that contains bioactive peptides of yellowfin tuna (<em>Thunnus albacares</em>) skin collagen with antioxidant activity has been successfully studied by using <em>in silico</em> and <em>in vitro</em> assays. We found that using the <em>in silico</em> assessment, the antioxidant peptides can be found from the precursor (type I α1 and α2 collagen of yellowfin tuna). Applying papain as a protease will also provide the greatest degree of hydrolysis for antioxidative peptides. The highest peptide rank peptides sequence such as Pro-Trp-Gly (PWG), Pro-His-Gly (PHG), His-Leu (HL), Ile-Arg (IR), Ala-His (AH), Glu-Leu (EL) that predicted using papain <em>in silico</em>. Molecular docking analysis showed all peptides derived from yellowfin tuna have hindered the substrate to access the active site of <em>myeloperoxidase</em> (MPO). Interestingly, the substitution of the amino acid from His (PHG, 7.1 kcal/mol) to Trp (PWG, 8.0 kcal/mol) has increased the affinity of the peptide towards MPO. They have antioxidative activities used <em>in silico</em> approach to MPO enzyme. We also confirm the <em>in vitro</em> assays for the protein hydrolysate after proteolysis using papain. The concentration and hydrolysis time will give influence the degree of hydrolysis, and antioxidant activities (<em>P</em> < 0.05). In conclusion, hydrolysate protein of type I α1 and α2 collagen from yellowfin tuna produced by papain hydrolysis has the potential to be used in food, active packaging material until health applications..</p></div>","PeriodicalId":12385,"journal":{"name":"Food Hydrocolloids for Health","volume":"3 ","pages":"Article 100126"},"PeriodicalIF":4.6000,"publicationDate":"2023-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"4","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Hydrocolloids for Health","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2667025923000110","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 4
Abstract
The protein hydrolysate that contains bioactive peptides of yellowfin tuna (Thunnus albacares) skin collagen with antioxidant activity has been successfully studied by using in silico and in vitro assays. We found that using the in silico assessment, the antioxidant peptides can be found from the precursor (type I α1 and α2 collagen of yellowfin tuna). Applying papain as a protease will also provide the greatest degree of hydrolysis for antioxidative peptides. The highest peptide rank peptides sequence such as Pro-Trp-Gly (PWG), Pro-His-Gly (PHG), His-Leu (HL), Ile-Arg (IR), Ala-His (AH), Glu-Leu (EL) that predicted using papain in silico. Molecular docking analysis showed all peptides derived from yellowfin tuna have hindered the substrate to access the active site of myeloperoxidase (MPO). Interestingly, the substitution of the amino acid from His (PHG, 7.1 kcal/mol) to Trp (PWG, 8.0 kcal/mol) has increased the affinity of the peptide towards MPO. They have antioxidative activities used in silico approach to MPO enzyme. We also confirm the in vitro assays for the protein hydrolysate after proteolysis using papain. The concentration and hydrolysis time will give influence the degree of hydrolysis, and antioxidant activities (P < 0.05). In conclusion, hydrolysate protein of type I α1 and α2 collagen from yellowfin tuna produced by papain hydrolysis has the potential to be used in food, active packaging material until health applications..