Antarctic fungus proteases generate bioactive peptides from caseinate

Detalhes bibliográficos
Autor(a) principal: Nascimento, Talita C.E.S.
Data de Publicação: 2021
Outros Autores: Molino, João Vitor Dutra, Donado, Priscila R.S., Montalvo, Gualberto S.A., dos Santos, Wellington L., Gomes, José Erick G. [UNESP], Santos, João H.P.M., da Silva, Roberto [UNESP], Sette, Lara Durães [UNESP], Pessoa Junior, Adalberto, Moreira, Keila Aparecida
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1016/j.foodres.2020.109944
http://hdl.handle.net/11449/207034
Resumo: The extracellular serine protease produced by Acremonium sp. L1-4B isolated from the Antarctic continent, was purified and used for the proteolysis of bovine and caprine sodium caseinate. Protein hydrolysates were evaluated in vitro to determine their antioxidant and antihypertensive potential, and later characterized by mass spectrometry. Bovine and caprine hydrolysates produced over 24 h showed a higher content of copper chelation (25.8 and 31.2% respectively), also at this time the ABTS+• scavenging was 65.2% (bovine sample) and 67.5% (caprine sample), and bovine caseinate hydrolysate (8 h) exhibited higher iron chelation capacity (43.1%). Statistically (p < 0.05), caprine caseinate hydrolysates showed relatively higher antioxidant potential in this study. All hydrolysates showed antihypertensive potential; however peptides released from caprine caseinate after 8 h of hydrolysis were able to inhibit 75% of angiotensin-converting enzyme (ACE) activity. Nano-ESI-Q-TOF-MS/MS analysis prospected a total of 23 different peptide sequences in the bovine hydrolysate fraction, originated from the αS1- and β-casein chain, whilst in caprine hydrolysate, 31 sequences were detected, all from β-casein. The low molecular weight bovine and caprine hydrolysates obtained in this research have the potential to act in the prevention of disorders caused by oxidative reactions and in the regulation of blood pressure. These findings support the development of new functional food and nutraceutical formulations.
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spelling Antarctic fungus proteases generate bioactive peptides from caseinateAngiotensin-converting enzymeAntarctic microorganismAntioxidant peptidesCow milkFunctional foodGoat milkHydrolysatesThe extracellular serine protease produced by Acremonium sp. L1-4B isolated from the Antarctic continent, was purified and used for the proteolysis of bovine and caprine sodium caseinate. Protein hydrolysates were evaluated in vitro to determine their antioxidant and antihypertensive potential, and later characterized by mass spectrometry. Bovine and caprine hydrolysates produced over 24 h showed a higher content of copper chelation (25.8 and 31.2% respectively), also at this time the ABTS+• scavenging was 65.2% (bovine sample) and 67.5% (caprine sample), and bovine caseinate hydrolysate (8 h) exhibited higher iron chelation capacity (43.1%). Statistically (p < 0.05), caprine caseinate hydrolysates showed relatively higher antioxidant potential in this study. All hydrolysates showed antihypertensive potential; however peptides released from caprine caseinate after 8 h of hydrolysis were able to inhibit 75% of angiotensin-converting enzyme (ACE) activity. Nano-ESI-Q-TOF-MS/MS analysis prospected a total of 23 different peptide sequences in the bovine hydrolysate fraction, originated from the αS1- and β-casein chain, whilst in caprine hydrolysate, 31 sequences were detected, all from β-casein. The low molecular weight bovine and caprine hydrolysates obtained in this research have the potential to act in the prevention of disorders caused by oxidative reactions and in the regulation of blood pressure. These findings support the development of new functional food and nutraceutical formulations.Department of Animal Morphology and Physiology Federal Rural University of PernambucoDepartment of Biochemical and Pharmaceutical Technology School of Pharmaceutical Sciences University of Sao PauloDepartment of Agribusiness Food and Nutrition ESALQ University of Sao PauloDepartment of Statistics and Applied Mathematics Federal University of CearáDepartment of Chemistry and Environmental Science IBILCE São Paulo State University (UNESP)Department of General and Applied Biology Institute of Biosciences São Paulo State University (UNESP)Federal University of Agreste of PernambucoDepartment of Chemistry and Environmental Science IBILCE São Paulo State University (UNESP)Department of General and Applied Biology Institute of Biosciences São Paulo State University (UNESP)Federal Rural University of PernambucoUniversidade de São Paulo (USP)Federal University of CearáUniversidade Estadual Paulista (Unesp)Federal University of Agreste of PernambucoNascimento, Talita C.E.S.Molino, João Vitor DutraDonado, Priscila R.S.Montalvo, Gualberto S.A.dos Santos, Wellington L.Gomes, José Erick G. [UNESP]Santos, João H.P.M.da Silva, Roberto [UNESP]Sette, Lara Durães [UNESP]Pessoa Junior, AdalbertoMoreira, Keila Aparecida2021-06-25T10:47:54Z2021-06-25T10:47:54Z2021-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://dx.doi.org/10.1016/j.foodres.2020.109944Food Research International, v. 139.1873-71450963-9969http://hdl.handle.net/11449/20703410.1016/j.foodres.2020.1099442-s2.0-85098451353Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengFood Research Internationalinfo:eu-repo/semantics/openAccess2021-10-23T16:01:11Zoai:repositorio.unesp.br:11449/207034Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T22:36:33.026558Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Antarctic fungus proteases generate bioactive peptides from caseinate
title Antarctic fungus proteases generate bioactive peptides from caseinate
spellingShingle Antarctic fungus proteases generate bioactive peptides from caseinate
Nascimento, Talita C.E.S.
Angiotensin-converting enzyme
Antarctic microorganism
Antioxidant peptides
Cow milk
Functional food
Goat milk
Hydrolysates
title_short Antarctic fungus proteases generate bioactive peptides from caseinate
title_full Antarctic fungus proteases generate bioactive peptides from caseinate
title_fullStr Antarctic fungus proteases generate bioactive peptides from caseinate
title_full_unstemmed Antarctic fungus proteases generate bioactive peptides from caseinate
title_sort Antarctic fungus proteases generate bioactive peptides from caseinate
author Nascimento, Talita C.E.S.
author_facet Nascimento, Talita C.E.S.
Molino, João Vitor Dutra
Donado, Priscila R.S.
Montalvo, Gualberto S.A.
dos Santos, Wellington L.
Gomes, José Erick G. [UNESP]
Santos, João H.P.M.
da Silva, Roberto [UNESP]
Sette, Lara Durães [UNESP]
Pessoa Junior, Adalberto
Moreira, Keila Aparecida
author_role author
author2 Molino, João Vitor Dutra
Donado, Priscila R.S.
Montalvo, Gualberto S.A.
dos Santos, Wellington L.
Gomes, José Erick G. [UNESP]
Santos, João H.P.M.
da Silva, Roberto [UNESP]
Sette, Lara Durães [UNESP]
Pessoa Junior, Adalberto
Moreira, Keila Aparecida
author2_role author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Federal Rural University of Pernambuco
Universidade de São Paulo (USP)
Federal University of Ceará
Universidade Estadual Paulista (Unesp)
Federal University of Agreste of Pernambuco
dc.contributor.author.fl_str_mv Nascimento, Talita C.E.S.
Molino, João Vitor Dutra
Donado, Priscila R.S.
Montalvo, Gualberto S.A.
dos Santos, Wellington L.
Gomes, José Erick G. [UNESP]
Santos, João H.P.M.
da Silva, Roberto [UNESP]
Sette, Lara Durães [UNESP]
Pessoa Junior, Adalberto
Moreira, Keila Aparecida
dc.subject.por.fl_str_mv Angiotensin-converting enzyme
Antarctic microorganism
Antioxidant peptides
Cow milk
Functional food
Goat milk
Hydrolysates
topic Angiotensin-converting enzyme
Antarctic microorganism
Antioxidant peptides
Cow milk
Functional food
Goat milk
Hydrolysates
description The extracellular serine protease produced by Acremonium sp. L1-4B isolated from the Antarctic continent, was purified and used for the proteolysis of bovine and caprine sodium caseinate. Protein hydrolysates were evaluated in vitro to determine their antioxidant and antihypertensive potential, and later characterized by mass spectrometry. Bovine and caprine hydrolysates produced over 24 h showed a higher content of copper chelation (25.8 and 31.2% respectively), also at this time the ABTS+• scavenging was 65.2% (bovine sample) and 67.5% (caprine sample), and bovine caseinate hydrolysate (8 h) exhibited higher iron chelation capacity (43.1%). Statistically (p < 0.05), caprine caseinate hydrolysates showed relatively higher antioxidant potential in this study. All hydrolysates showed antihypertensive potential; however peptides released from caprine caseinate after 8 h of hydrolysis were able to inhibit 75% of angiotensin-converting enzyme (ACE) activity. Nano-ESI-Q-TOF-MS/MS analysis prospected a total of 23 different peptide sequences in the bovine hydrolysate fraction, originated from the αS1- and β-casein chain, whilst in caprine hydrolysate, 31 sequences were detected, all from β-casein. The low molecular weight bovine and caprine hydrolysates obtained in this research have the potential to act in the prevention of disorders caused by oxidative reactions and in the regulation of blood pressure. These findings support the development of new functional food and nutraceutical formulations.
publishDate 2021
dc.date.none.fl_str_mv 2021-06-25T10:47:54Z
2021-06-25T10:47:54Z
2021-01-01
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.foodres.2020.109944
Food Research International, v. 139.
1873-7145
0963-9969
http://hdl.handle.net/11449/207034
10.1016/j.foodres.2020.109944
2-s2.0-85098451353
url http://dx.doi.org/10.1016/j.foodres.2020.109944
http://hdl.handle.net/11449/207034
identifier_str_mv Food Research International, v. 139.
1873-7145
0963-9969
10.1016/j.foodres.2020.109944
2-s2.0-85098451353
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Food Research International
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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