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

被引：73

作者：

Drummond e Silva, Fernanda Guimaraes ^{[1
]}

Hernandez-Ledesma, Blanca ^{[2
]}

Amigo, Lourdes ^{[2
]}

Netto, Flavia Maria ^{[1
]}

Miralles, Beatriz ^{[2
]}

机构：

[1] Univ Estadual Campinas, UNICAMP, Fac Food Engn, Monteiro Lobato 80, BR-80130838 Campinas, SP, Brazil

[2] UAM, CSIC, Inst Invest Ciencias Alimentac, CIAL,CEI, Nicolas Cabrera 9, Madrid 28049, Spain

来源：

LWT-FOOD SCIENCE AND TECHNOLOGY | 2017年 / 76卷

基金：

巴西圣保罗研究基金会;

关键词：

Flaxseed; Peptides; Antioxidant capacity; Alcalase (R) hydrolysis; Tandem mass spectrometry; IN-VITRO; BETA-LACTOGLOBULIN; L; PROTEIN; FRACTIONS; CAPACITY;

D O I：

10.1016/j.lwt.2016.10.049

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

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.

引用

页码：140 / 146

页数：7

共 36 条

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