Antarctic fungus proteases generate bioactive peptides from caseinate
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , , , , , |
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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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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1808129442533343232 |