Antarctic fungus proteases generate bioactive peptides from caseinate
| Autor: | Lara Durães Sette, José Erick Galindo Gomes, João H. P. M. Santos, Priscila Robertina dos Santos Donado, Talita Camila Evaristo da Silva Nascimento, Roberto da Silva, Adalberto Pessoa Junior, João Vitor Dutra Molino, Gualberto S. A Montalvo, Wellington Leal dos Santos, Keila Aparecida Moreira |
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| Přispěvatelé: | Federal Rural University of Pernambuco, Universidade de São Paulo (USP), Federal University of Ceará, Universidade Estadual Paulista (Unesp), Federal University of Agreste of Pernambuco |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Proteases
Antioxidant Goat milk Cow milk 030309 nutrition & dietetics Proteolysis medicine.medical_treatment Angiotensin-Converting Enzyme Inhibitors Hydrolysate Antioxidant peptides 03 medical and health sciences chemistry.chemical_compound 0404 agricultural biotechnology Tandem Mass Spectrometry medicine Extracellular Animals Food science Serine protease 0303 health sciences ABTS biology medicine.diagnostic_test Chemistry Goats PROTEINASES Functional food Fungi Caseins 04 agricultural and veterinary sciences Copper Chelation Hydrolysates 040401 food science biology.protein Cattle Peptides Antarctic microorganism Angiotensin-converting enzyme Peptide Hydrolases Food Science |
| Zdroj: | Scopus Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| Popis: | Made available in DSpace on 2021-06-25T10:47:54Z (GMT). No. of bitstreams: 0 Previous issue date: 2021-01-01 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. Department of Animal Morphology and Physiology Federal Rural University of Pernambuco Department of Biochemical and Pharmaceutical Technology School of Pharmaceutical Sciences University of Sao Paulo Department of Agribusiness Food and Nutrition ESALQ University of Sao Paulo Department of Statistics and Applied Mathematics Federal University of Ceará Department 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 Pernambuco Department 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) |
| Databáze: | OpenAIRE |
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