dc.creatorDrummond e Silva
dc.creatorFernanda Guimaraes; Hernandez-Ledesma
dc.creatorBlanca; Amigo
dc.creatorLourdes; Netto
dc.creatorFlavia Maria; Miralles
dc.creatorBeatriz
dc.date2017
dc.datemar
dc.date2017-11-13T11:33:04Z
dc.date2017-11-13T11:33:04Z
dc.date.accessioned2018-03-29T05:47:36Z
dc.date.available2018-03-29T05:47:36Z
dc.identifierLwt-food Science And Technology. Elsevier Science Bv, v. 76, p. 140 - 146, 2017.
dc.identifier0023-6438
dc.identifier1096-1127
dc.identifierWOS:000390726400018
dc.identifier10.1016/j.lwt.2016.10.049
dc.identifierhttp://www.sciencedirect.com/science/article/pii/S002364381630651X?via%3Dihub
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/326200
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1363206
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionIn 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.
dc.description76
dc.description140
dc.description146
dc.descriptionFAPESP [2010/52680-7]
dc.descriptionCNPq
dc.descriptionMinistry of Economy and Competitiveness (MINECO)
dc.description[AGL2015-66886-R]
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.languageEnglish
dc.publisherElsevier Science BV
dc.publisherAmsterdam
dc.relationLWT-Food Science and Technology
dc.rightsfechado
dc.sourceWOS
dc.subjectFlaxseed
dc.subjectPeptides
dc.subjectAntioxidant Capacity
dc.subjectAlcalase (r) Hydrolysis
dc.subjectTandem Mass Spectrometry
dc.titleIdentification Of Peptides Released From Flaxseed (linum Usitatissimum) Protein By Alcalase (r) Hydrolysis: Antioxidant Activity
dc.typeArtículos de revistas


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