Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions

Detalhes bibliográficos
Autor(a) principal: Santos, Wellington Leal dos
Data de Publicação: 2020
Outros Autores: Silva, Thailan Arlindo da, Nascimento, Patrícia Lins Azevedo do, Falcão, Rosângela Estevão Alves, Oliveira, João Tiago Correia, Moreira, Keila Aparecida
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Research, Society and Development
Texto Completo: https://rsdjournal.org/index.php/rsd/article/view/10772
Resumo: In the present study, buffalo milk caseinate hydrolysates produced by bromelain, neutrase, papain and trypsin were ultra-filtered and different fractions were assessed for antioxidant, inhibition of angiotensin converting enzyme and antimicrobial activity. Biological potential was assessed by a number of metrics: ability to remove radicals of 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid), 2,2'-diphenyl-1-picrylhydrazyl (DPPH) and hydroxyls; copper and iron chelation; antidiabetic properties; antihypertensive assay; and antibacterial activity against Escherichia coli ATCC 25922, Listeria monocytogenes ATCC 19114, Salmonella typhimurium ATCC 14028 and Staphylococcus aureus ATCC 25923 strains. The tests for scavenging of hydroxyl radicals and DPPH revealed a greater potential in the 3–10 kDa fractions. Iron chelation activity >70% was observed in all the fractions, including <3 kDa. Copper chelation was >60% in fractions >10 kDa. α-Amylase inhibition and antihypertensive activity was optimal in the <3 kDa fraction. Antibacterial activity ranged between 3.28 and 100% inhibition against microorganisms tested, the fraction <3 kDa showed a greater inhibitory potential.  The antihypertensive activity of fractions ranged between 39.35 and 89.58%. All treatments were able to produce hydrolysates and fractions with biological potential and, so the ultrafiltration method proved to be effective in the separation of peptides with different molar masses and potential use in the food or pharmaceutical industry.
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spelling Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractionsActividad antioxidante, inhibición de la enzima convertidora de angiotensina I (ECA) y actividad antibacteriana de hidrolizados de proteína de caseinato de búfalo y sus fracciones Atividade antioxidante, inibição da enzima conversora de angiotensina I (ECA) e atividade antibacteriana de hidrolisados proteicos de caseinato de búfalo e suas fraçõesUltrafiltraçãoLeite de búfaloAlimentos funcionais.UltrafiltraciónLeche de búfaloAlimentos funcionales.UltrafiltrationBuffalo milkFunctional food.In the present study, buffalo milk caseinate hydrolysates produced by bromelain, neutrase, papain and trypsin were ultra-filtered and different fractions were assessed for antioxidant, inhibition of angiotensin converting enzyme and antimicrobial activity. Biological potential was assessed by a number of metrics: ability to remove radicals of 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid), 2,2'-diphenyl-1-picrylhydrazyl (DPPH) and hydroxyls; copper and iron chelation; antidiabetic properties; antihypertensive assay; and antibacterial activity against Escherichia coli ATCC 25922, Listeria monocytogenes ATCC 19114, Salmonella typhimurium ATCC 14028 and Staphylococcus aureus ATCC 25923 strains. The tests for scavenging of hydroxyl radicals and DPPH revealed a greater potential in the 3–10 kDa fractions. Iron chelation activity >70% was observed in all the fractions, including <3 kDa. Copper chelation was >60% in fractions >10 kDa. α-Amylase inhibition and antihypertensive activity was optimal in the <3 kDa fraction. Antibacterial activity ranged between 3.28 and 100% inhibition against microorganisms tested, the fraction <3 kDa showed a greater inhibitory potential.  The antihypertensive activity of fractions ranged between 39.35 and 89.58%. All treatments were able to produce hydrolysates and fractions with biological potential and, so the ultrafiltration method proved to be effective in the separation of peptides with different molar masses and potential use in the food or pharmaceutical industry.En el presente estudio, los caseinatos de leche de búfala producidos por bromelina, neutrasa, papaína y tripsina fueron ultrafiltrados y se evaluó la actividad antioxidante y antimicrobiana de diferentes fracciones. El potencial biológico se evaluó mediante una serie de mediciones: capacidad de eliminar los radicales del 2,2'-azino-bis (ácido 3-etilbenctiazolín-6-sulfónico), 2,2'-difenil-1-picrilhidrazilo (DPPH) e hidroxilos; quelación del cobre y el hierro; propiedades antidiabéticas; inhibición de la enzima convertidora de angiotensina; y actividad antibacteriana contra las cepas de Escherichia coli ATCC 25922, Listeria monocytogenes ATCC 19114, Salmonella typhimurium ATCC 14028 y Staphylococcus aureus ATCC 25923. Las pruebas de eliminación de radicales hidroxilo y DPPH revelaron un mayor potencial en las fracciones de 3-10 kDa. Se observó una actividad de quelación del hierro >70% en todas las fracciones, incluyendo <3 kDa. La quelación del cobre fue >60% en las fracciones >10 kDa. α La inhibición de la amilasa y la actividad antihipertensiva fue óptima en la fracción <3 kDa. La actividad antibacteriana osciló entre 3,28 y 100% de inhibición contra los microorganismos probados, la fracción <3 kDa mostró un mayor potencial inhibitorio.  La actividad antihipertensiva de las fracciones osciló entre el 39,35 y el 89,58%. Todos los tratamientos fueron capaces de producir hidrolizados y fracciones con potencial biológico, por lo que el método de ultrafiltración demostró ser eficaz en la separación de péptidos con diferentes masas molares y su posible uso en la industria alimentaria o farmacéutica.No presente estudo, os hidrolisados do caseinato de leite de búfala produzidos por bromelina, neutrase, papaína e tripsina foram ultrafiltrados, e diferentes frações foram avaliadas quanto à atividade antioxidante, inibição da enzima conversora de angiotensina I e antimicrobiana. O potencial biológico foi avaliado através de uma série de atividades: capacidade de remover radicais de 2,2'-azino-bis (ácido 3-etilbenztiazolina-6-sulfônico), 2,2'-difenil-1-picrylhydrazyl (DPPH) e hidroxilas; quelação de cobre e ferro; propriedades antidiabéticas; inibição da enzima conversora de angiotensina; e atividade antibacteriana contra Escherichia coli ATCC 25922, Listeria monocytogenes ATCC 19114, Salmonella typhimurium ATCC 14028 e cepas de Staphylococcus aureus ATCC 25923. Os testes para sequestro dos radicais hidroxila e DPPH revelaram um maior potencial nas frações de 3-10 kDa. A atividade de quelação do ferro >70% foi observada em todas as frações, incluindo <3 kDa.  A quelação do cobre foi >60% nas frações >10 kDa.  A inibição da α-amilase e atividade anti-hipertensiva foi ótima na fração <3 kDa. A atividade antibacteriana variou entre 3,28 e 100% de inibição contra os microrganismos testados. A fração <3 kDa mostrou um potencial inibitório maior.  A atividade anti-hipertensiva das frações variou entre 39,35 e 89,58%. Todos os tratamentos foram capazes de produzir hidrolisados e frações com potencial biológico e, portanto, o método de ultrafiltração prova ser eficaz na separação de peptídeos com diferentes massas molares e uso potencial na indústria alimentícia ou farmacêutica.Research, Society and Development2020-12-24info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://rsdjournal.org/index.php/rsd/article/view/1077210.33448/rsd-v9i12.10772Research, Society and Development; Vol. 9 No. 12; e27591210772Research, Society and Development; Vol. 9 Núm. 12; e27591210772Research, Society and Development; v. 9 n. 12; e275912107722525-3409reponame:Research, Society and Developmentinstname:Universidade Federal de Itajubá (UNIFEI)instacron:UNIFEIenghttps://rsdjournal.org/index.php/rsd/article/view/10772/9920Copyright (c) 2020 Wellington Leal dos Santos; Thailan Arlindo da Silva; Patrícia Lins Azevedo do Nascimento; Rosângela Estevão Alves Falcão; João Tiago Correia Oliveira; Keila Aparecida Moreirahttps://creativecommons.org/licenses/by/4.0info:eu-repo/semantics/openAccessSantos, Wellington Leal dos Silva, Thailan Arlindo daNascimento, Patrícia Lins Azevedo do Falcão, Rosângela Estevão Alves Oliveira, João Tiago Correia Moreira, Keila Aparecida 2020-12-30T23:32:22Zoai:ojs.pkp.sfu.ca:article/10772Revistahttps://rsdjournal.org/index.php/rsd/indexPUBhttps://rsdjournal.org/index.php/rsd/oairsd.articles@gmail.com2525-34092525-3409opendoar:2024-01-17T09:32:45.859695Research, Society and Development - Universidade Federal de Itajubá (UNIFEI)false
dc.title.none.fl_str_mv Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions
Actividad antioxidante, inhibición de la enzima convertidora de angiotensina I (ECA) y actividad antibacteriana de hidrolizados de proteína de caseinato de búfalo y sus fracciones
Atividade antioxidante, inibição da enzima conversora de angiotensina I (ECA) e atividade antibacteriana de hidrolisados proteicos de caseinato de búfalo e suas frações
title Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions
spellingShingle Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions
Santos, Wellington Leal dos
Ultrafiltração
Leite de búfalo
Alimentos funcionais.
Ultrafiltración
Leche de búfalo
Alimentos funcionales.
Ultrafiltration
Buffalo milk
Functional food.
title_short Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions
title_full Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions
title_fullStr Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions
title_full_unstemmed Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions
title_sort Antioxidant activity, inhibition of angiotensin I converting enzyme (ACE) and antibacterial activity of buffalo caseinate protein hydrolysates and their fractions
author Santos, Wellington Leal dos
author_facet Santos, Wellington Leal dos
Silva, Thailan Arlindo da
Nascimento, Patrícia Lins Azevedo do
Falcão, Rosângela Estevão Alves
Oliveira, João Tiago Correia
Moreira, Keila Aparecida
author_role author
author2 Silva, Thailan Arlindo da
Nascimento, Patrícia Lins Azevedo do
Falcão, Rosângela Estevão Alves
Oliveira, João Tiago Correia
Moreira, Keila Aparecida
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Santos, Wellington Leal dos
Silva, Thailan Arlindo da
Nascimento, Patrícia Lins Azevedo do
Falcão, Rosângela Estevão Alves
Oliveira, João Tiago Correia
Moreira, Keila Aparecida
dc.subject.por.fl_str_mv Ultrafiltração
Leite de búfalo
Alimentos funcionais.
Ultrafiltración
Leche de búfalo
Alimentos funcionales.
Ultrafiltration
Buffalo milk
Functional food.
topic Ultrafiltração
Leite de búfalo
Alimentos funcionais.
Ultrafiltración
Leche de búfalo
Alimentos funcionales.
Ultrafiltration
Buffalo milk
Functional food.
description In the present study, buffalo milk caseinate hydrolysates produced by bromelain, neutrase, papain and trypsin were ultra-filtered and different fractions were assessed for antioxidant, inhibition of angiotensin converting enzyme and antimicrobial activity. Biological potential was assessed by a number of metrics: ability to remove radicals of 2,2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid), 2,2'-diphenyl-1-picrylhydrazyl (DPPH) and hydroxyls; copper and iron chelation; antidiabetic properties; antihypertensive assay; and antibacterial activity against Escherichia coli ATCC 25922, Listeria monocytogenes ATCC 19114, Salmonella typhimurium ATCC 14028 and Staphylococcus aureus ATCC 25923 strains. The tests for scavenging of hydroxyl radicals and DPPH revealed a greater potential in the 3–10 kDa fractions. Iron chelation activity >70% was observed in all the fractions, including <3 kDa. Copper chelation was >60% in fractions >10 kDa. α-Amylase inhibition and antihypertensive activity was optimal in the <3 kDa fraction. Antibacterial activity ranged between 3.28 and 100% inhibition against microorganisms tested, the fraction <3 kDa showed a greater inhibitory potential.  The antihypertensive activity of fractions ranged between 39.35 and 89.58%. All treatments were able to produce hydrolysates and fractions with biological potential and, so the ultrafiltration method proved to be effective in the separation of peptides with different molar masses and potential use in the food or pharmaceutical industry.
publishDate 2020
dc.date.none.fl_str_mv 2020-12-24
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://rsdjournal.org/index.php/rsd/article/view/10772
10.33448/rsd-v9i12.10772
url https://rsdjournal.org/index.php/rsd/article/view/10772
identifier_str_mv 10.33448/rsd-v9i12.10772
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv https://rsdjournal.org/index.php/rsd/article/view/10772/9920
dc.rights.driver.fl_str_mv https://creativecommons.org/licenses/by/4.0
info:eu-repo/semantics/openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/4.0
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Research, Society and Development
publisher.none.fl_str_mv Research, Society and Development
dc.source.none.fl_str_mv Research, Society and Development; Vol. 9 No. 12; e27591210772
Research, Society and Development; Vol. 9 Núm. 12; e27591210772
Research, Society and Development; v. 9 n. 12; e27591210772
2525-3409
reponame:Research, Society and Development
instname:Universidade Federal de Itajubá (UNIFEI)
instacron:UNIFEI
instname_str Universidade Federal de Itajubá (UNIFEI)
instacron_str UNIFEI
institution UNIFEI
reponame_str Research, Society and Development
collection Research, Society and Development
repository.name.fl_str_mv Research, Society and Development - Universidade Federal de Itajubá (UNIFEI)
repository.mail.fl_str_mv rsd.articles@gmail.com
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