Purification and identification of antioxidative peptides from loach ( Misgurnus anguillicaudatus) protein hydrolysate by consecutive chromatography and electrospray ionization-mass spectrometry

Loach protein was hydrolyzed by papain to obtain antioxidative peptides. The results showed that the loach protein hydrolysate (LPH) could scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) (IC 50 = 17.0 ± 0.54 mg/mL) and hydroxyl radicals (IC 50 = 2.64 ± 0.29 mg/mL). It could chelate cupric ion and inhi...

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Bibliographic Details
Published in:Food research international 2010-05, Vol.43 (4), p.1167-1173
Main Authors: You, Lijun, Zhao, Mouming, Regenstein, Joe M., Ren, Jiaoyan
Format: Article
Language:English
Subjects:
antioxidant activity
antioxidants
Antioxidative peptides
Biological and medical sciences
chelating activity
chelation
Chromatography
CORROSION PROTECTION
Electrospray ionization-mass spectrometry
emulsions
fish protein hydrolysate
Food industries
free radical scavengers
freshwater fish
Fundamental and applied biological sciences. Psychology
gel permeation chromatography
Hydrolysates
Hydroxyl radical scavenging activity
Hydroxyl radicals
ion exchange chromatography
Ionization
linoleic acid
lipid peroxidation
Liquid chromatography
Loach ( Misgurnus anguillicaudatus)
mass spectrometry
Misgurnus anguillicaudatus
oil-water interface
ORGANIC COMPOUNDS
Peptides
protein isolates
Proteins
PURIFICATION
Radical scavenging activity
reversed-phase high performance liquid chromatography
SPRAYING
ultrafiltration
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Summary:Loach protein was hydrolyzed by papain to obtain antioxidative peptides. The results showed that the loach protein hydrolysate (LPH) could scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) (IC 50 = 17.0 ± 0.54 mg/mL) and hydroxyl radicals (IC 50 = 2.64 ± 0.29 mg/mL). It could chelate cupric ion and inhibit the lipid peroxidation in a linoleic acid emulsion system. The hydrolysate was isolated and purified by ultrafiltration and consecutive chromatographic methods including ion-exchange chromatography, gel filtration chromatography and a two-step reverse high-performance liquid chromatography (RP-HPLC). The purified antioxidant peptide was identified as Pro-Ser-Tyr-Val (464.2 Da) using RP-HPLC connected on-line to an electrospray ionization (ESI) mass spectrometer. The purified peptide showed a 9.14-fold higher scavenging activity for hydroxyl radical compared with the crude LPH. Therefore, it is possible to produce natural antioxidative peptides from loach protein by enzymatic hydrolysis and purification.
ISSN:0963-9969
1873-7145
DOI:10.1016/j.foodres.2010.02.009