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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Published in:Food Research International
Main Authors: 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
Other Authors: Universidade Estadual Paulista (UNESP)
Format: Article in Journal/Newspaper
Language:English
Published: 2021
Subjects:
Online Access:http://hdl.handle.net/11449/207034
https://doi.org/10.1016/j.foodres.2020.109944
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record_format openpolar
spelling 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
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