Identification of peptides released from flaxseed (linum usitatissimum) protein by alcalase(R) hydrolysis: antioxidant activity

In this study, the hydrolysis of a flaxseed protein isolate with Alcalase® was performed as a strategy to generate antioxidant peptides. A chromatographic separation of the hydrolysate was conducted by RP-HPLC. Both hydrolysate and six collected fractions were subjected to ORAC and FRAP assays to evaluate their antioxidant capacity. The higher antioxidant values were shown by fractions containing predominantly low molecular weight peptides, as it was demonstrated by MALDI analysis. Four peptides were identified by LC-MS/MS and one by Edman degradation. The peptide with sequence GFPGRLDHWCASE was synthesised showing a notable ORAC activity, 3.20 μmol Trolox equivalents/μmol of peptide. This value was higher than that reported for butylated hydroxyanisole. Therefore, the contribution of this peptide to the activity of the fraction where it had been found was 61%. The identified sequences represent an advance in the molecular characterization of the flaxseed protein fraction76A140146CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICO - CNPQFUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULO - FAPESPSem informação2010/52680-

Identification Of Peptides Released From Flaxseed (linum Usitatissimum) Protein By Alcalase (r) Hydrolysis: Antioxidant Activity

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)In this study, the hydrolysis of a flaxseed protein isolate with Alcalase (R) was performed as a strategy to generate antioxidant peptides. A chromatographic separation of the hydrolysate was conducted by RPHPLC. Both hydrolysate and six collected fractions were subjected to ORAC and FRAP assays to evaluate their antioxidant capacity. The higher antioxidant values were shown by fractions containing predominantly low molecular weight peptides, as it was demonstrated by MALDI analysis. Four peptides were identified by LC-MS/MS and one by Edman degradation. The peptide with sequence GFPGRLDHWCASE was synthesised showing a notable ORAC activity, 3.20 mu mol Trolox equivalents/mu mol of peptide. This value was higher than that reported for butylated hydroxyanisole. Therefore, the contribution of this peptide to the activity of the fraction where it had been found was 61%. The identified sequences represent an advance in the molecular characterization of the flaxseed protein fraction. (C) 2016 Elsevier Ltd. All rights reserved.76140146FAPESP [2010/52680-7]CNPqMinistry of Economy and Competitiveness (MINECO)[AGL2015-66886-R]Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq

Identification of peptides released from flaxseed (Linum usitatissimum) protein by Alcalase® hydrolysis: Antioxidant activity

In this study, the hydrolysis of a flaxseed protein isolate with Alcalase was performed as a strategy to generate antioxidant peptides. A chromatographic separation of the hydrolysate was conducted by RP-HPLC. Both hydrolysate and six collected fractions were subjected to ORAC and FRAP assays to evaluate their antioxidant capacity. The higher antioxidant values were shown by fractions containing predominantly low molecular weight peptides, as it was demonstrated by MALDI analysis. Four peptides were identified by LC-MS/MS and one by Edman degradation. The peptide with sequence GFPGRLDHWCASE was synthesised showing a notable ORAC activity, 3.20 μmol Trolox equivalents/μmol of peptide. This value was higher than that reported for butylated hydroxyanisole. Therefore, the contribution of this peptide to the activity of the fraction where it had been found was 61%. The identified sequences represent an advance in the molecular characterization of the flaxseed protein fraction.This work has received financial support from projects AGL2015-66886-R and FAPESP (2010/52680-7). F.G.D. Silva acknowledges the CNPq for the scholarship granted, and B. Hernández-Ledesma thanks the Ministry of Economy and Competitiveness (MINECO) for her “Ramón y Cajal” post-doctoral contract.Peer Reviewe