Identification of novel antioxidative peptides derived from a thermolytic Hydrolysate of ovotransferrin by LC-MS/MS

Gwen Shen, Baljot Chahal, Kaustav Majumder, Sun Jong You, Jianping Wu

Research output: Contribution to journalArticle

64 Citations (Scopus)

Abstract

Ovotransferrin is a glycoprotein well-known for its iron-binding property. Ovotransferrin was reported to have antioxidative properties, but the presence of antioxidant peptides within the protein has not been reported. The purpose of the study was to characterize the antioxidant peptides within ovotransferrin. Ovotransferrin was sonicated and hydrolyzed by thermolysin, and peptides from the hydrolysate were fractionated by ion-exchange fast protein liquid chromatography and reversed-phase high-performance liquid chromatography. Fourteen peptides derived from ovotransferrin were characterized using LC-MS/MS, and their oxygen radical absorbance capacity (ORAC) values were determined using synthetic peptides. Two tetrapeptides (Trp-Asn-lle-Pro and Gly-Trp-Asn-lle) showed the highest antioxidant activity. Interestingly, the addition of amino acid residues to either the N or C terminus of the two peptides decreased the antioxidant activity, suggesting that the motif of Trp-Asn-lle is responsible for the high antioxidant activity.

Original languageEnglish (US)
Pages (from-to)7664-7672
Number of pages9
JournalJournal of Agricultural and Food Chemistry
Volume58
Issue number13
DOIs
StatePublished - Jul 14 2010

Fingerprint

Conalbumin
hydrolysates
peptides
Antioxidants
Peptides
antioxidant activity
antioxidants
oxygen radical absorbance capacity
binding properties
Thermolysin
synthetic peptides
reversed-phase high performance liquid chromatography
ion exchange
Ion Exchange
Liquid chromatography
liquid chromatography
High performance liquid chromatography
Reverse-Phase Chromatography
glycoproteins
Liquid Chromatography

Keywords

  • Antioxidant peptides
  • LC-MS/MS
  • Ovotransferrin
  • Thermolysin

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

Cite this

Identification of novel antioxidative peptides derived from a thermolytic Hydrolysate of ovotransferrin by LC-MS/MS. / Shen, Gwen; Chahal, Baljot; Majumder, Kaustav; You, Sun Jong; Wu, Jianping.

In: Journal of Agricultural and Food Chemistry, Vol. 58, No. 13, 14.07.2010, p. 7664-7672.

Research output: Contribution to journalArticle

@article{8235c38dd2154e14a46f9a68f5769284,
title = "Identification of novel antioxidative peptides derived from a thermolytic Hydrolysate of ovotransferrin by LC-MS/MS",
abstract = "Ovotransferrin is a glycoprotein well-known for its iron-binding property. Ovotransferrin was reported to have antioxidative properties, but the presence of antioxidant peptides within the protein has not been reported. The purpose of the study was to characterize the antioxidant peptides within ovotransferrin. Ovotransferrin was sonicated and hydrolyzed by thermolysin, and peptides from the hydrolysate were fractionated by ion-exchange fast protein liquid chromatography and reversed-phase high-performance liquid chromatography. Fourteen peptides derived from ovotransferrin were characterized using LC-MS/MS, and their oxygen radical absorbance capacity (ORAC) values were determined using synthetic peptides. Two tetrapeptides (Trp-Asn-lle-Pro and Gly-Trp-Asn-lle) showed the highest antioxidant activity. Interestingly, the addition of amino acid residues to either the N or C terminus of the two peptides decreased the antioxidant activity, suggesting that the motif of Trp-Asn-lle is responsible for the high antioxidant activity.",
keywords = "Antioxidant peptides, LC-MS/MS, Ovotransferrin, Thermolysin",
author = "Gwen Shen and Baljot Chahal and Kaustav Majumder and You, {Sun Jong} and Jianping Wu",
year = "2010",
month = "7",
day = "14",
doi = "10.1021/jf101323y",
language = "English (US)",
volume = "58",
pages = "7664--7672",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "13",

}

TY - JOUR

T1 - Identification of novel antioxidative peptides derived from a thermolytic Hydrolysate of ovotransferrin by LC-MS/MS

AU - Shen, Gwen

AU - Chahal, Baljot

AU - Majumder, Kaustav

AU - You, Sun Jong

AU - Wu, Jianping

PY - 2010/7/14

Y1 - 2010/7/14

N2 - Ovotransferrin is a glycoprotein well-known for its iron-binding property. Ovotransferrin was reported to have antioxidative properties, but the presence of antioxidant peptides within the protein has not been reported. The purpose of the study was to characterize the antioxidant peptides within ovotransferrin. Ovotransferrin was sonicated and hydrolyzed by thermolysin, and peptides from the hydrolysate were fractionated by ion-exchange fast protein liquid chromatography and reversed-phase high-performance liquid chromatography. Fourteen peptides derived from ovotransferrin were characterized using LC-MS/MS, and their oxygen radical absorbance capacity (ORAC) values were determined using synthetic peptides. Two tetrapeptides (Trp-Asn-lle-Pro and Gly-Trp-Asn-lle) showed the highest antioxidant activity. Interestingly, the addition of amino acid residues to either the N or C terminus of the two peptides decreased the antioxidant activity, suggesting that the motif of Trp-Asn-lle is responsible for the high antioxidant activity.

AB - Ovotransferrin is a glycoprotein well-known for its iron-binding property. Ovotransferrin was reported to have antioxidative properties, but the presence of antioxidant peptides within the protein has not been reported. The purpose of the study was to characterize the antioxidant peptides within ovotransferrin. Ovotransferrin was sonicated and hydrolyzed by thermolysin, and peptides from the hydrolysate were fractionated by ion-exchange fast protein liquid chromatography and reversed-phase high-performance liquid chromatography. Fourteen peptides derived from ovotransferrin were characterized using LC-MS/MS, and their oxygen radical absorbance capacity (ORAC) values were determined using synthetic peptides. Two tetrapeptides (Trp-Asn-lle-Pro and Gly-Trp-Asn-lle) showed the highest antioxidant activity. Interestingly, the addition of amino acid residues to either the N or C terminus of the two peptides decreased the antioxidant activity, suggesting that the motif of Trp-Asn-lle is responsible for the high antioxidant activity.

KW - Antioxidant peptides

KW - LC-MS/MS

KW - Ovotransferrin

KW - Thermolysin

UR - http://www.scopus.com/inward/record.url?scp=77954558977&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77954558977&partnerID=8YFLogxK

U2 - 10.1021/jf101323y

DO - 10.1021/jf101323y

M3 - Article

C2 - 20568771

AN - SCOPUS:77954558977

VL - 58

SP - 7664

EP - 7672

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 13

ER -