Taurine, homotaurine, GABA and hydrophobic amino acids content influences “in vitro” antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates from algae

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.

Document Type

Article

Document version

Published version

Language

English

Pages

14

Publisher

Nature Research

Published in

Scientific Reports

Grant Agreement Number

EC/H2020/862980/EU/MICROALGAE PROTEIN INGREDIENTS FOR THE FOOD AND FEED OF THE FUTURE/ProFuture

Recommended citation

Terriente-Palacios, Carlos, Susana Rubiño, Maria Hortós, César Peteiro, and Massimo Castellari. 2022. "Taurine, Homotaurine, GABA And Hydrophobic Amino Acids Content Influences “In Vitro” Antioxidant And SIRT1 Modulation Activities Of Enzymatic Protein Hydrolysates From Algae". Scientific Reports 12 (1). doi:10.1038/s41598-022-25130-4.

Rights

Attribution 4.0 International

Attribution 4.0 International

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