Purification and characterization of antioxidant peptide from sunflower protein hydrolysate

Sunflower proteins were hydrolyzed with Flavourzyme for the production of antioxidant peptide. DEAE-Sepharose Fast Flow, Sephadex G-25 gel filtration chromatography and reversed-phase HPLC were consecutively employed to purify a novel sunflower antioxidant peptide, and the ability to inhibit the aut...

Full description

Saved in:
Bibliographic Details
Published in:Food Technology and Biotechnology 2010, Vol.48 (4), p.519
Main Authors: Ren, Jian, Zheng, Xi-Qun, Liu, Xiao-Lan, Liu, Huan
Format: Report
Language:English
Subjects:
Antioxidants
Chemical properties
Composition
Identification and classification
Peptides
Production processes
Protein hydrolysates
Sunflower seed oil
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page
container_issue 4
container_start_page 519
container_title Food Technology and Biotechnology
container_volume 48
creator Ren, Jian
Zheng, Xi-Qun
Liu, Xiao-Lan
Liu, Huan
description Sunflower proteins were hydrolyzed with Flavourzyme for the production of antioxidant peptide. DEAE-Sepharose Fast Flow, Sephadex G-25 gel filtration chromatography and reversed-phase HPLC were consecutively employed to purify a novel sunflower antioxidant peptide, and the ability to inhibit the autoxidation of pyrogallol was expressed as the antioxidative activity of the peptide. The amino acid sequence was identified as Ala-Cys-Ala-His-Asp-Lys-Val by a Q-Tof2 mass spectrometer. This novel peptide exhibited a high antioxidative activity of 79.42 U/mL, which is expected to protect against oxidative damage in living systems in relation to aging and carcinogenesis. Higher antioxidative activities were presumed mainly due to the presence of hydrophobic amino acids in its sequence.
format report
fullrecord <record><control><sourceid>gale</sourceid><recordid>TN_cdi_gale_infotracmisc_A248659712</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A248659712</galeid><sourcerecordid>A248659712</sourcerecordid><originalsourceid>FETCH-gale_infotracmisc_A2486597123</originalsourceid><addsrcrecordid>eNqNjbsKwjAYRjMoWC_vEHAutI32Mooojg5uDhKSP_aXNClJitanN6AP4HQ-Dge-CUlyxrK0qctiRubeP7KM1VWTJ-R6HhwqFDygNZQbSUXLHRcBHL6_0qro43qhjKQ99AElUOVsR_1glLZPcLR3NgAa2o7SWT16HmBJpoprD6sfF2R9PFz2p_TONdzQKBviU4de3HbFpi63TZUX7L_qA9UaQ8I</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>report</recordtype></control><display><type>report</type><title>Purification and characterization of antioxidant peptide from sunflower protein hydrolysate</title><source>EBSCOHost: Business Source Ultimate</source><creator>Ren, Jian ; Zheng, Xi-Qun ; Liu, Xiao-Lan ; Liu, Huan</creator><creatorcontrib>Ren, Jian ; Zheng, Xi-Qun ; Liu, Xiao-Lan ; Liu, Huan</creatorcontrib><description>Sunflower proteins were hydrolyzed with Flavourzyme for the production of antioxidant peptide. DEAE-Sepharose Fast Flow, Sephadex G-25 gel filtration chromatography and reversed-phase HPLC were consecutively employed to purify a novel sunflower antioxidant peptide, and the ability to inhibit the autoxidation of pyrogallol was expressed as the antioxidative activity of the peptide. The amino acid sequence was identified as Ala-Cys-Ala-His-Asp-Lys-Val by a Q-Tof2 mass spectrometer. This novel peptide exhibited a high antioxidative activity of 79.42 U/mL, which is expected to protect against oxidative damage in living systems in relation to aging and carcinogenesis. Higher antioxidative activities were presumed mainly due to the presence of hydrophobic amino acids in its sequence.</description><identifier>ISSN: 1330-9862</identifier><language>eng</language><publisher>Sveuciliste U Zagrebu</publisher><subject>Antioxidants ; Chemical properties ; Composition ; Identification and classification ; Peptides ; Production processes ; Protein hydrolysates ; Sunflower seed oil</subject><ispartof>Food Technology and Biotechnology, 2010, Vol.48 (4), p.519</ispartof><rights>COPYRIGHT 2010 Sveuciliste U Zagrebu</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>776,780,4476</link.rule.ids></links><search><creatorcontrib>Ren, Jian</creatorcontrib><creatorcontrib>Zheng, Xi-Qun</creatorcontrib><creatorcontrib>Liu, Xiao-Lan</creatorcontrib><creatorcontrib>Liu, Huan</creatorcontrib><title>Purification and characterization of antioxidant peptide from sunflower protein hydrolysate</title><title>Food Technology and Biotechnology</title><description>Sunflower proteins were hydrolyzed with Flavourzyme for the production of antioxidant peptide. DEAE-Sepharose Fast Flow, Sephadex G-25 gel filtration chromatography and reversed-phase HPLC were consecutively employed to purify a novel sunflower antioxidant peptide, and the ability to inhibit the autoxidation of pyrogallol was expressed as the antioxidative activity of the peptide. The amino acid sequence was identified as Ala-Cys-Ala-His-Asp-Lys-Val by a Q-Tof2 mass spectrometer. This novel peptide exhibited a high antioxidative activity of 79.42 U/mL, which is expected to protect against oxidative damage in living systems in relation to aging and carcinogenesis. Higher antioxidative activities were presumed mainly due to the presence of hydrophobic amino acids in its sequence.</description><subject>Antioxidants</subject><subject>Chemical properties</subject><subject>Composition</subject><subject>Identification and classification</subject><subject>Peptides</subject><subject>Production processes</subject><subject>Protein hydrolysates</subject><subject>Sunflower seed oil</subject><issn>1330-9862</issn><fulltext>true</fulltext><rsrctype>report</rsrctype><creationdate>2010</creationdate><recordtype>report</recordtype><sourceid/><recordid>eNqNjbsKwjAYRjMoWC_vEHAutI32Mooojg5uDhKSP_aXNClJitanN6AP4HQ-Dge-CUlyxrK0qctiRubeP7KM1VWTJ-R6HhwqFDygNZQbSUXLHRcBHL6_0qro43qhjKQ99AElUOVsR_1glLZPcLR3NgAa2o7SWT16HmBJpoprD6sfF2R9PFz2p_TONdzQKBviU4de3HbFpi63TZUX7L_qA9UaQ8I</recordid><startdate>20101001</startdate><enddate>20101001</enddate><creator>Ren, Jian</creator><creator>Zheng, Xi-Qun</creator><creator>Liu, Xiao-Lan</creator><creator>Liu, Huan</creator><general>Sveuciliste U Zagrebu</general><scope/></search><sort><creationdate>20101001</creationdate><title>Purification and characterization of antioxidant peptide from sunflower protein hydrolysate</title><author>Ren, Jian ; Zheng, Xi-Qun ; Liu, Xiao-Lan ; Liu, Huan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-gale_infotracmisc_A2486597123</frbrgroupid><rsrctype>reports</rsrctype><prefilter>reports</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Antioxidants</topic><topic>Chemical properties</topic><topic>Composition</topic><topic>Identification and classification</topic><topic>Peptides</topic><topic>Production processes</topic><topic>Protein hydrolysates</topic><topic>Sunflower seed oil</topic><toplevel>online_resources</toplevel><creatorcontrib>Ren, Jian</creatorcontrib><creatorcontrib>Zheng, Xi-Qun</creatorcontrib><creatorcontrib>Liu, Xiao-Lan</creatorcontrib><creatorcontrib>Liu, Huan</creatorcontrib></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ren, Jian</au><au>Zheng, Xi-Qun</au><au>Liu, Xiao-Lan</au><au>Liu, Huan</au><format>book</format><genre>unknown</genre><ristype>RPRT</ristype><atitle>Purification and characterization of antioxidant peptide from sunflower protein hydrolysate</atitle><jtitle>Food Technology and Biotechnology</jtitle><date>2010-10-01</date><risdate>2010</risdate><volume>48</volume><issue>4</issue><spage>519</spage><pages>519-</pages><issn>1330-9862</issn><abstract>Sunflower proteins were hydrolyzed with Flavourzyme for the production of antioxidant peptide. DEAE-Sepharose Fast Flow, Sephadex G-25 gel filtration chromatography and reversed-phase HPLC were consecutively employed to purify a novel sunflower antioxidant peptide, and the ability to inhibit the autoxidation of pyrogallol was expressed as the antioxidative activity of the peptide. The amino acid sequence was identified as Ala-Cys-Ala-His-Asp-Lys-Val by a Q-Tof2 mass spectrometer. This novel peptide exhibited a high antioxidative activity of 79.42 U/mL, which is expected to protect against oxidative damage in living systems in relation to aging and carcinogenesis. Higher antioxidative activities were presumed mainly due to the presence of hydrophobic amino acids in its sequence.</abstract><pub>Sveuciliste U Zagrebu</pub></addata></record>
fulltext fulltext
identifier ISSN: 1330-9862
ispartof Food Technology and Biotechnology, 2010, Vol.48 (4), p.519
issn 1330-9862
language eng
recordid cdi_gale_infotracmisc_A248659712
source EBSCOHost: Business Source Ultimate
subjects Antioxidants
Chemical properties
Composition
Identification and classification
Peptides
Production processes
Protein hydrolysates
Sunflower seed oil
title Purification and characterization of antioxidant peptide from sunflower protein hydrolysate
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-23T15%3A51%3A15IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale&rft_val_fmt=info:ofi/fmt:kev:mtx:book&rft.genre=unknown&rft.atitle=Purification%20and%20characterization%20of%20antioxidant%20peptide%20from%20sunflower%20protein%20hydrolysate&rft.jtitle=Food%20Technology%20and%20Biotechnology&rft.au=Ren,%20Jian&rft.date=2010-10-01&rft.volume=48&rft.issue=4&rft.spage=519&rft.pages=519-&rft.issn=1330-9862&rft_id=info:doi/&rft_dat=%3Cgale%3EA248659712%3C/gale%3E%3Cgrp_id%3Ecdi_FETCH-gale_infotracmisc_A2486597123%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rft_galeid=A248659712&rfr_iscdi=true