Antarctic fungus proteases generate bioactive peptides from caseinate

Autor(es):Mostrar menos -

Nascimento, Talita C. E. S. ^[1] ; Dutra Molino, Joao Vitor ^[2] ; Donado, Priscila R. S. ^[3] ; Montalvo, Gualberto S. A. ^[4] ; dos Santos, Wellington L. ^[1] ; Gomes, Jose Erick G. ^[5] ; Santos, Joao H. P. M. ^[2] ; da Silva, Roberto ^[5] ; Sette, Lara Duraes ^[6] ; Pessoa Junior, Adalberto ^[2] ; Moreira, Keila Aparecida ^[7]

Afiliação do(s) autor(es)

^[1] Univ Fed Rural Pernambuco, Dept Anim Morphol & Physiol, Recife, PE - Brazil

^[2] Univ Sao Paulo, Sch Pharmaceut Sci, Dept Biochem & Pharmaceut Technol, Sao Paulo, SP - Brazil

^[3] Univ Sao Paulo, Dept Agribusiness Food & Nutr, ESALQ, Piracicaba, SP - Brazil

^[4] Univ Fed Ceara, Dept Stat & Appl Math, Fortaleza, Ceara - Brazil

^[5] Sao Paulo State Univ UNESP, Dept Chem & Environm Sci, IBILCE, Sao Jose Do Rio Preto, SP - Brazil

^[6] Sao Paulo State Univ UNESP, Inst Biosci, Dept Gen & Appl Biol, Rio Claro - Brazil

^[7] Fed Univ Agreste Pernambuco, Garanhuns, PE - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Food Research International; v. 139, JAN 2021.
• Citações Web of Science: 0

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(+center dot) 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 alpha S1- and beta-casein chain, whilst in caprine hydrolysate, 31 sequences were detected, all from beta-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. (AU)

• Processo FAPESP: 10/17033-0 - Exploração biotecnológica de fungos derivados da Antártica
• Beneficiário: Lara Durães Sette
• Modalidade de apoio: Auxílio à Pesquisa - Regular