Antioxidative peptides derived from denaturated egg white protein
Aleksandra Zambrowicz , Marta Pokora , Ewelina Eckert , Józefa Chrzanowska , Marek Szołtysik , Anna Dąbrowska , Tadeusz Trziszka
The antioxidant activity of denaturated egg white protein preparation (EP) was evaluated by enzymatic hydrolysis. The EP treated with digestive and microbial proteases resulted in different degradation products confirmed by degree of hydrolysis (DH) and free amino groups concentration (FAG) measurement. The highest free radical scavenging activity reached 0.21 μmol troloxeq/mg and was exhibited by tryptic hydrolysate. EP hydrolysates showed significant, enzyme-dependent ferric reducing activity. The highest chelating activity was observed for protein preparations hydrolyzed with neutrase (397.0 μg Fe2+/mg). Antioxidative peptide fractions were isolated from tryptic hydrolysate by reserved phase high pressure liquid chromatography (RP-HPLC). Among the obtained fractions, we identified: ISQAVHAHAEINEAGR, SVL, QL and AP, KVR antioxidative peptides corresponded to ovalbumin and ovotransferrin fragments, respectively.
|Journal series||Italian Journal of Food Science, ISSN 1120-1770, (A 15 pkt)|
|Keywords in English||Antioxidant, DPPH, Hydrolysis, Ovalbumin, Peptide|
|Score|| = 15.0, 09-09-2020, ArticleFromJournal|
= 15.0, 09-09-2020, ArticleFromJournal
|Publication indicators||= 5; = 5; : 2013 = 0.22; : 2013 = 0.2 (2) - 2013=0.309 (5)|
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