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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

Okara is a solid byproduct created during the processing of soy milk. The production of protein hydrolysates utilizing enzymatic tests such as papain can result in the production of bioactive peptides (BPs), which are amino acid sequences that can also be produced from the okara protein by hydrolysis. The objective of this study was to investigate the antioxidant activities of okara hydrolysates using papain, based on the in silico and in vitro assays using the papain enzyme. We found that using the in silico assessment, the antioxidant peptides can be found from the precursor (glycinin and conglycinin) in okara. When used as a protease, papain provides the maximum degree of hydrolysis for antioxidative peptides. The highest-peptide-rank peptide sequence was predicted using peptide ranks such as proline–histidine–phenylalanine (PHF), alanine–aspartic acid–phenylalanine (ADF), tyrosine–tyrosine–leucine (YYL), proline–histidine–histidine (PHH), isoleucine–arginine (IR), and serine–valine–leucine (SVL). Molecular docking studies revealed that all peptides generated from the parent protein impeded substrate access to the active site of xanthine oxidase (XO). They have antioxidative properties and are employed in the in silico approach to the XO enzyme. We also use papain to evaluate the antioxidant activity by using in vitro tests for protein hydrolysate following proteolysis. The antioxidant properties of okara protein hydrolysates have been shown in vitro, utilizing DPPH and FRAP experiments. This study suggests that okara hydrolysates generated by papain can be employed as natural antioxidants in food and for further applications, such as active ingredients for antioxidants in packaging.