Cargando…

Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction

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 hydrolysi...

Descripción completa

Detalles Bibliográficos
Autores principales: Ningrum, Andriati, Wardani, Dian Wahyu, Vanidia, Nurul, Manikharda, Sarifudin, Achmat, Kumalasari, Rima, Ekafitri, Riyanti, Kristanti, Dita, Setiaboma, Woro, Munawaroh, Heli Siti Helimatul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10343360/
https://www.ncbi.nlm.nih.gov/pubmed/37446636
http://dx.doi.org/10.3390/molecules28134974
_version_ 1785072718490632192
author Ningrum, Andriati
Wardani, Dian Wahyu
Vanidia, Nurul
Manikharda
Sarifudin, Achmat
Kumalasari, Rima
Ekafitri, Riyanti
Kristanti, Dita
Setiaboma, Woro
Munawaroh, Heli Siti Helimatul
author_facet Ningrum, Andriati
Wardani, Dian Wahyu
Vanidia, Nurul
Manikharda
Sarifudin, Achmat
Kumalasari, Rima
Ekafitri, Riyanti
Kristanti, Dita
Setiaboma, Woro
Munawaroh, Heli Siti Helimatul
author_sort Ningrum, Andriati
collection PubMed
description 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.
format Online
Article
Text
id pubmed-10343360
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-103433602023-07-14 Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction Ningrum, Andriati Wardani, Dian Wahyu Vanidia, Nurul Manikharda Sarifudin, Achmat Kumalasari, Rima Ekafitri, Riyanti Kristanti, Dita Setiaboma, Woro Munawaroh, Heli Siti Helimatul Molecules Article 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. MDPI 2023-06-24 /pmc/articles/PMC10343360/ /pubmed/37446636 http://dx.doi.org/10.3390/molecules28134974 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Ningrum, Andriati
Wardani, Dian Wahyu
Vanidia, Nurul
Manikharda
Sarifudin, Achmat
Kumalasari, Rima
Ekafitri, Riyanti
Kristanti, Dita
Setiaboma, Woro
Munawaroh, Heli Siti Helimatul
Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction
title Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction
title_full Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction
title_fullStr Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction
title_full_unstemmed Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction
title_short Evaluation of Antioxidant Activities from a Sustainable Source of Okara Protein Hydrolysate Using Enzymatic Reaction
title_sort evaluation of antioxidant activities from a sustainable source of okara protein hydrolysate using enzymatic reaction
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10343360/
https://www.ncbi.nlm.nih.gov/pubmed/37446636
http://dx.doi.org/10.3390/molecules28134974
work_keys_str_mv AT ningrumandriati evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction
AT wardanidianwahyu evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction
AT vanidianurul evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction
AT manikharda evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction
AT sarifudinachmat evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction
AT kumalasaririma evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction
AT ekafitririyanti evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction
AT kristantidita evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction
AT setiabomaworo evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction
AT munawarohhelisitihelimatul evaluationofantioxidantactivitiesfromasustainablesourceofokaraproteinhydrolysateusingenzymaticreaction