Antarctic fungus proteases generate bioactive peptides from caseinate

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MetadadosDescriçãoIdioma
Autor(es): dc.contributorFederal Rural University of Pernambuco-
Autor(es): dc.contributorUniversidade de São Paulo (USP)-
Autor(es): dc.contributorFederal University of Ceará-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorFederal University of Agreste of Pernambuco-
Autor(es): dc.creatorNascimento, Talita C.E.S.-
Autor(es): dc.creatorMolino, João Vitor Dutra-
Autor(es): dc.creatorDonado, Priscila R.S.-
Autor(es): dc.creatorMontalvo, Gualberto S.A.-
Autor(es): dc.creatordos Santos, Wellington L.-
Autor(es): dc.creatorGomes, José Erick G. [UNESP]-
Autor(es): dc.creatorSantos, João H.P.M.-
Autor(es): dc.creatorda Silva, Roberto [UNESP]-
Autor(es): dc.creatorSette, Lara Durães [UNESP]-
Autor(es): dc.creatorPessoa Junior, Adalberto-
Autor(es): dc.creatorMoreira, Keila Aparecida-
Data de aceite: dc.date.accessioned2022-02-22T00:49:00Z-
Data de disponibilização: dc.date.available2022-02-22T00:49:00Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2020-12-31-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1016/j.foodres.2020.109944-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/207034-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/207034-
Descrição: dc.descriptionThe 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.-
Descrição: dc.descriptionDepartment of Animal Morphology and Physiology Federal Rural University of Pernambuco-
Descrição: dc.descriptionDepartment of Biochemical and Pharmaceutical Technology School of Pharmaceutical Sciences University of Sao Paulo-
Descrição: dc.descriptionDepartment of Agribusiness Food and Nutrition ESALQ University of Sao Paulo-
Descrição: dc.descriptionDepartment of Statistics and Applied Mathematics Federal University of Ceará-
Descrição: dc.descriptionDepartment of Chemistry and Environmental Science IBILCE São Paulo State University (UNESP)-
Descrição: dc.descriptionDepartment of General and Applied Biology Institute of Biosciences São Paulo State University (UNESP)-
Descrição: dc.descriptionFederal University of Agreste of Pernambuco-
Descrição: dc.descriptionDepartment of Chemistry and Environmental Science IBILCE São Paulo State University (UNESP)-
Descrição: dc.descriptionDepartment of General and Applied Biology Institute of Biosciences São Paulo State University (UNESP)-
Idioma: dc.languageen-
Relação: dc.relationFood Research International-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectAngiotensin-converting enzyme-
Palavras-chave: dc.subjectAntarctic microorganism-
Palavras-chave: dc.subjectAntioxidant peptides-
Palavras-chave: dc.subjectCow milk-
Palavras-chave: dc.subjectFunctional food-
Palavras-chave: dc.subjectGoat milk-
Palavras-chave: dc.subjectHydrolysates-
Título: dc.titleAntarctic fungus proteases generate bioactive peptides from caseinate-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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