Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance

Xinyan Peng; Youling L. Xiong; Baohua Kong

doi:10.1016/j.foodchem.2008.07.068

Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance

Xinyan Peng, Youling L. Xiong, Baohua Kong

Animal and Food Sciences

Research output: Contribution to journal › Article › peer-review

242 Scopus citations

Abstract

Whey protein isolate (WPI) was hydrolysed for 0.5-8 h using Alcalase, and the 5-h hydrolysate, identified to possess the strongest reducing ability, was subjected to column fractionation and antioxidant activity assays. Sephadex G-10 gel filtration chromatography of the 5-h hydrolysate yielded four fractions (I, II, III and IV) that were composed of peptides of >40k, 2.8-40k, 0.1-2.8k, and <0.1k, respectively. Fraction III exhibited the strongest free radical scavenging effects, which was evidenced by the electron spin resonance (ESR) of 1,1-diphenyl-2-picrylhydrazyl radicals (DPPH^{{radical dot}}) and of trapped hydroxyl (^{{radical dot}}OH) and superoxide (O₂^{{radical dot} -}) radicals. The results indicated that antioxidant activity of whey protein hydrolysates depended on peptide molecular weight, with peptides of 0.1-2.8k possessing the strongest radical scavenging activity.

Original language	English
Pages (from-to)	196-201
Number of pages	6
Journal	Food Chemistry
Volume	113
Issue number	1
DOIs	https://doi.org/10.1016/j.foodchem.2008.07.068
State	Published - Mar 1 2009

Bibliographical note

Funding Information:
This study was a joint project between Northeast Agricultural University (China) and University of Kentucky (USA), which was supported by a grant from the Natural Science Foundation of Heilongjiang Province for overseas collaboration (Grant No. ZJN0605-01), and by a grant from the 863 Plan of Ministry of Science and Technology of China (Grant No. 2008AA10Z315).

Keywords

Antioxidant activity
Antioxidant peptide
Electron spin resonance
Whey protein isolates

ASJC Scopus subject areas

Analytical Chemistry
Food Science

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10.1016/j.foodchem.2008.07.068

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title = "Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance",

abstract = "Whey protein isolate (WPI) was hydrolysed for 0.5-8 h using Alcalase, and the 5-h hydrolysate, identified to possess the strongest reducing ability, was subjected to column fractionation and antioxidant activity assays. Sephadex G-10 gel filtration chromatography of the 5-h hydrolysate yielded four fractions (I, II, III and IV) that were composed of peptides of >40k, 2.8-40k, 0.1-2.8k, and <0.1k, respectively. Fraction III exhibited the strongest free radical scavenging effects, which was evidenced by the electron spin resonance (ESR) of 1,1-diphenyl-2-picrylhydrazyl radicals (DPPH{radical dot}) and of trapped hydroxyl ({radical dot}OH) and superoxide (O2{radical dot} -) radicals. The results indicated that antioxidant activity of whey protein hydrolysates depended on peptide molecular weight, with peptides of 0.1-2.8k possessing the strongest radical scavenging activity.",

keywords = "Antioxidant activity, Antioxidant peptide, Electron spin resonance, Whey protein isolates",

author = "Xinyan Peng and Xiong, {Youling L.} and Baohua Kong",

note = "Funding Information: This study was a joint project between Northeast Agricultural University (China) and University of Kentucky (USA), which was supported by a grant from the Natural Science Foundation of Heilongjiang Province for overseas collaboration (Grant No. ZJN0605-01), and by a grant from the 863 Plan of Ministry of Science and Technology of China (Grant No. 2008AA10Z315).",

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AU - Peng, Xinyan

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AU - Kong, Baohua

N1 - Funding Information: This study was a joint project between Northeast Agricultural University (China) and University of Kentucky (USA), which was supported by a grant from the Natural Science Foundation of Heilongjiang Province for overseas collaboration (Grant No. ZJN0605-01), and by a grant from the 863 Plan of Ministry of Science and Technology of China (Grant No. 2008AA10Z315).

PY - 2009/3/1

Y1 - 2009/3/1

N2 - Whey protein isolate (WPI) was hydrolysed for 0.5-8 h using Alcalase, and the 5-h hydrolysate, identified to possess the strongest reducing ability, was subjected to column fractionation and antioxidant activity assays. Sephadex G-10 gel filtration chromatography of the 5-h hydrolysate yielded four fractions (I, II, III and IV) that were composed of peptides of >40k, 2.8-40k, 0.1-2.8k, and <0.1k, respectively. Fraction III exhibited the strongest free radical scavenging effects, which was evidenced by the electron spin resonance (ESR) of 1,1-diphenyl-2-picrylhydrazyl radicals (DPPH{radical dot}) and of trapped hydroxyl ({radical dot}OH) and superoxide (O2{radical dot} -) radicals. The results indicated that antioxidant activity of whey protein hydrolysates depended on peptide molecular weight, with peptides of 0.1-2.8k possessing the strongest radical scavenging activity.

AB - Whey protein isolate (WPI) was hydrolysed for 0.5-8 h using Alcalase, and the 5-h hydrolysate, identified to possess the strongest reducing ability, was subjected to column fractionation and antioxidant activity assays. Sephadex G-10 gel filtration chromatography of the 5-h hydrolysate yielded four fractions (I, II, III and IV) that were composed of peptides of >40k, 2.8-40k, 0.1-2.8k, and <0.1k, respectively. Fraction III exhibited the strongest free radical scavenging effects, which was evidenced by the electron spin resonance (ESR) of 1,1-diphenyl-2-picrylhydrazyl radicals (DPPH{radical dot}) and of trapped hydroxyl ({radical dot}OH) and superoxide (O2{radical dot} -) radicals. The results indicated that antioxidant activity of whey protein hydrolysates depended on peptide molecular weight, with peptides of 0.1-2.8k possessing the strongest radical scavenging activity.

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Antioxidant activity of peptide fractions from whey protein hydrolysates as measured by electron spin resonance

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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