Repozytorium

Multifunctional peptides derived from an egg yolk protein hydrolysate : isolation and characterization.

Autorzy

Aleksandra Zambrowicz

Marta Pokora

Bartosz Setner

Anna Dąbrowska

Marek Szołtysik

Konrad Babij

Zbigniew Szewczuk

Tadeusz Trziszka

Gert Lubec

Józefa Chrzanowska

Rok wydania

2015

Czasopismo

Amino Acids

Numer woluminu

47

Strony

369-380

DOI

10.1007/s00726-014-1869-x

Kolekcja

Naukowa

Język

Angielski

Typ publikacji

Artykuł

Streszczenie

An egg yolk protein by-product following ethanol extraction of phospholipids (YP) was hydrolyzed with pepsin to produce and identify novel peptides that revealed antioxidant, ACE inhibitory and antidiabetic (α-glucosidase and DPP-IV inhibitory) activities. The peptic hydrolysate of YP was fractionated by ion-exchange chromatography and reversedphase high-pressure liquid chromatography. Isolated peptides were identified using mass spectrometry (MALDI-ToF) and the Mascot Search Results database. Four peptides of MW ranging from 1,210.62 to 1,677.88 Da corresponded to the fragments of Apolipoprotein B (YINQMPQKSRE; YINQMPQKSREA), Vitellogenin-2 (VTGRFAGHPAAQ) and Apovitellenin-1 (YIEAVNKVSPRAGQF). These peptides were chemically synthesized and showed antioxidant, ACE inhibitory or/and antidiabetic activities. Peptide YIEAVNKVSPRAGQF exerted the strongest ACE inhibitory activity, with IC50 = 9.4 µg/mL. The peptide YINQMPQKSRE showed the strongest DPPH free radical scavenging and DPP-IV inhibitory activities and its ACE inhibitory activity (IC50) reached 10.1 µg/mL. The peptide VTGRFAGHPAAQ revealed the highest α-glucosidase inhibitory activity (IC50 = 365.4 µg/mL). A novel nutraceutical effect for peptides from an egg yolk hydrolysate was shown.

Słowa kluczowe

Egg yolk protein by-product, Hydrolysis, Antioxidant, Antidiabetic, Angiotensin I-converting enzyme inhibitory activity

Licencja otwartego dostępu

CC-BY

Licencja na prawach której można swobodnie kopiować, rozprowadzać, zmieniać i remiksować objęty prawem autorskim utwór (Utwór-przedmiot prawa autorskiego) pod warunkiem podania imienia i nazwiska autora utworu pierwotnego oraz źródła pochodzenia utworu.

Pełny tekst licencji: https://creativecommons.org/licenses/by/3.0/pl/legalcode

Adres publiczny

http://dx.doi.org/10.1007/s00726-014-1869-x

Strona internetowa wydawcy

http://link.springer.com

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