Antarctic fungus proteases generate bioactive peptides from caseinate
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...
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Online Access: | http://hdl.handle.net/11449/207034 https://doi.org/10.1016/j.foodres.2020.109944 |
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ftunivespir:oai:repositorio.unesp.br:11449/207034 2023-07-02T03:30:01+02:00 Antarctic fungus proteases generate bioactive peptides from caseinate 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. Santos, João H.P.M. da Silva, Roberto Sette, Lara Durães Pessoa Junior, Adalberto Moreira, Keila Aparecida Universidade Estadual Paulista (UNESP) 2021-01-01 http://hdl.handle.net/11449/207034 https://doi.org/10.1016/j.foodres.2020.109944 eng eng Food Research International 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 doi:10.1016/j.foodres.2020.109944 2-s2.0-85098451353 Angiotensin-converting enzyme Antarctic microorganism Antioxidant peptides Cow milk Functional food Goat milk Hydrolysates info:eu-repo/semantics/article 2021 ftunivespir https://doi.org/10.1016/j.foodres.2020.109944 2023-06-12T17:26:22Z 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. Article in Journal/Newspaper Antarc* Antarctic Universidade Estadual Paulista São Paulo: Repositório Institucional UNESP Antarctic The Antarctic Food Research International 139 109944 |
institution |
Open Polar |
collection |
Universidade Estadual Paulista São Paulo: Repositório Institucional UNESP |
op_collection_id |
ftunivespir |
language |
English |
topic |
Angiotensin-converting enzyme Antarctic microorganism Antioxidant peptides Cow milk Functional food Goat milk Hydrolysates |
spellingShingle |
Angiotensin-converting enzyme Antarctic microorganism Antioxidant peptides Cow milk Functional food Goat milk Hydrolysates 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. Santos, João H.P.M. da Silva, Roberto Sette, Lara Durães Pessoa Junior, Adalberto Moreira, Keila Aparecida Antarctic fungus proteases generate bioactive peptides from caseinate |
topic_facet |
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. |
author2 |
Universidade Estadual Paulista (UNESP) |
format |
Article in Journal/Newspaper |
author |
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. Santos, João H.P.M. da Silva, Roberto Sette, Lara Durães Pessoa Junior, Adalberto Moreira, Keila Aparecida |
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. Santos, João H.P.M. da Silva, Roberto Sette, Lara Durães Pessoa Junior, Adalberto Moreira, Keila Aparecida |
author_sort |
Nascimento, Talita C.E.S. |
title |
Antarctic fungus proteases generate bioactive peptides from caseinate |
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 |
publishDate |
2021 |
url |
http://hdl.handle.net/11449/207034 https://doi.org/10.1016/j.foodres.2020.109944 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
Food Research International 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 doi:10.1016/j.foodres.2020.109944 2-s2.0-85098451353 |
op_doi |
https://doi.org/10.1016/j.foodres.2020.109944 |
container_title |
Food Research International |
container_volume |
139 |
container_start_page |
109944 |
_version_ |
1770274271346556928 |