Isolation and characterization of free radical scavenging activities peptides derived from casein

Isolation and characterization of free radical scavenging activities peptides derived from casein A peptide having the strong free radical scavenging activities was separated from casein protein hydrolysate by chromatographic analyses such as ion-exchange and gel filtration. SP-II fraction obtained by SP-Sephadex C-25 chromatography showed the most potent superoxide anion scavenging activity (SOSA), and it was further separated into a peptide using an octadecylsilano-high performance liquid chromatography. The amino acid sequence of the peptide was Tyr-Phe-Tyr-Pro-Glu-Leu (YFYPEL). The concentration of the test compound required to reduce the produced superoxide anion to one-half (IC 50 ) value for SOSA was 79.2 μM using tetrazolium salt 3′-{1-((phenylamino)-carbonyl)-3,4-tetrazolium}-bis(4-methoxy-6-nitro)benzenesulfonic acid hydrate method. The IC 50 value for the 1,1-diphenyl-2-picrylhydrazyl radical and hydroxyl radical scavenging activities were 98 and 251 μM, respectively, based on the electron spin resonance method. We characterized SOSA of the C-terminal sequence using EL, PEL, YPEL, and FYPEL. The activities of preferred sequences were EL > YFYPEL > FYPEL > YPEL > PEL, suggesting that the Glu-Leu sequence is important for the activity. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Nutritional Biochemistry Elsevier

Isolation and characterization of free radical scavenging activities peptides derived from casein

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Publisher
Elsevier
Copyright
Copyright © 2000 Elsevier Science Inc.
ISSN
0955-2863
D.O.I.
10.1016/S0955-2863(99)00083-2
Publisher site
See Article on Publisher Site

Abstract

A peptide having the strong free radical scavenging activities was separated from casein protein hydrolysate by chromatographic analyses such as ion-exchange and gel filtration. SP-II fraction obtained by SP-Sephadex C-25 chromatography showed the most potent superoxide anion scavenging activity (SOSA), and it was further separated into a peptide using an octadecylsilano-high performance liquid chromatography. The amino acid sequence of the peptide was Tyr-Phe-Tyr-Pro-Glu-Leu (YFYPEL). The concentration of the test compound required to reduce the produced superoxide anion to one-half (IC 50 ) value for SOSA was 79.2 μM using tetrazolium salt 3′-{1-((phenylamino)-carbonyl)-3,4-tetrazolium}-bis(4-methoxy-6-nitro)benzenesulfonic acid hydrate method. The IC 50 value for the 1,1-diphenyl-2-picrylhydrazyl radical and hydroxyl radical scavenging activities were 98 and 251 μM, respectively, based on the electron spin resonance method. We characterized SOSA of the C-terminal sequence using EL, PEL, YPEL, and FYPEL. The activities of preferred sequences were EL > YFYPEL > FYPEL > YPEL > PEL, suggesting that the Glu-Leu sequence is important for the activity.

Journal

The Journal of Nutritional BiochemistryElsevier

Published: Mar 1, 2000

References

  • Isolation and characterization of angiotensin I-converting enzyme inhibitor dipeptides derived from Allium sativum L (GARLIC)
    Suetsuna, K.

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