Abstract

Prevention and control of diseases and delaying the signs of ageing are nowadays one of the major goals of biomedicine. Sirtuins, a family of NAD+ dependent deacylase enzymes, could be pivotal targets of novel preventive and therapeutic strategies to achieve such aims. SIRT1 activating and inhibiting compounds, such as polyphenols and bioactive peptides, have been proposed to be involved in the development of many human diseases. The objective of this work was to assess and compare the antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates (EPHs) from a wide number of algae species (24 commercial samples and 12 samples harvested off the Atlantic coast of northern Spain). High antioxidant activities were observed in EPHs from red and green seaweed species. Moreover, 19 samples exhibited SIRT1 activation, while EPHs from the 16 samples were SIRT1 inhibitors. Pearson's correlation test and Principal Component Analysis revealed significant correlations between (1) total peptide and hydrophobic amino acid content in EPHs and their antioxidant activities, and (2) concentrations of taurine, homotaurine, and amino acid gamma aminobutyric acid in EPHs and their SIRT1 modulation activity.

Details

Title
Taurine, homotaurine, GABA and hydrophobic amino acids content influences “in vitro” antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates from algae
Author
Terriente-Palacios, Carlos 1 ; Rubiño, Susana 2 ; Hortós, Maria 2 ; Peteiro, César 3 ; Castellari, Massimo 2 

 IRTA, Food Safety and Functionality Programe, Girona, Spain; Escuela Internacional de Doctorado de la Universidad Nacional de Educación a Distancia (EIDUNED), Madrid, Spain (GRID:grid.10702.34) (ISNI:0000 0001 2308 8920) 
 IRTA, Food Safety and Functionality Programe, Girona, Spain (GRID:grid.10702.34) 
 Seaweeds Center, Spanish Institute of Oceanography of the Spanish National Research Council (IEO, CSIC), Oceanographic Center of Santander, Marine Culture Units “El Bocal”, Santander, Spain (GRID:grid.10702.34) 
Publication year
2022
Publication date
2022
Publisher
Nature Publishing Group
e-ISSN
20452322
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2745196622
Copyright
© The Author(s) 2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.