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contributor authorH. Tanzadehpanahen
contributor authorاحمد آسودهen
contributor authorJ. Chamanien
contributor authorAhmad Asoodehfa
date accessioned2020-06-06T13:09:17Z
date available2020-06-06T13:09:17Z
date issued2012
identifier urihttps://libsearch.um.ac.ir:443/fum/handle/fum/3343736?locale-attribute=en&show=full
description abstractOstrich (Struthio camelus) egg white (OEW) proteinswere hydrolyzed using various proteases (α-chymotrypsin,

pepsin, trypsin and papain). Antioxidant activities of hydrolysates were evaluated using 1, 1-diphenyl-

2-picrylhydrazyl (DPPH) radical scavenging and iron chelating activity. The hydrolysate obtained by trypsin

exhibited the highest antioxidant activity. This hydrolysate was passed through an ultrafiltration membrane

with a 3 kDa-cut off, and the resulting filtrate was purified using reversed-phase high performance liquid

chromatography (RP-HPLC). Eight peptide fractions were separated and their antioxidant activities were tested.

The results showed that the F6 fraction possessed the highest antioxidant activity in the inhibition of linoleic acid

autoxidation (86.4% at 20 μg/ml), scavenging activity for DPPH radical (81% at 200 μg/ml) and 2, 2-azino-bis

(3-ethylbenzothiazoline-6-sulphonicacid) diammonium salt (ABTS) radical (37.6% at 90.9 μg/ml). In addition,

the iron chelating activity, hydroxyl radical scavenging and reducing power of the F6 fraction were 20% at

317.5 μg/ml, 28.6% at 163.9 μg/ml and 0.083 at 113.6 μg/ml, respectively. The peptide sequence was found to

be LTEQESGVPVMK (with a molecular mass of 1317.65 Da) using mass spectrometry. The results suggest that

the digestion of OEWproteins by trypsin protease could be exploited to produce natural antioxidants.
en
languageEnglish
titleAn antioxidant peptide derived from Ostrich (Struthio camelus) egg white protein hydrolysatesen
typeJournal Paper
contenttypeExternal Fulltext
subject keywordsOstrich egg white hydrolysates

Antioxidant activity

Bioactive peptide

Mass spectrometry
en
journal titleFood Research Internationalfa
pages105-111
journal volume49
journal issue1
identifier linkhttps://profdoc.um.ac.ir/paper-abstract-1029602.html
identifier articleid1029602


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