1. Multifunctional peptides derived from an egg yolk protein hydrolysate: isolation and characterization
- Author
-
Józefa Chrzanowska, Anna Dąbrowska, Bartosz Setner, Tadeusz Trziszka, Aleksandra Zambrowicz, Marek Szołtysik, Konrad Babij, Marta Pokora, Zbigniew Szewczuk, and Gert Lubec
- Subjects
food.ingredient ,Antioxidant ,Saccharomyces cerevisiae Proteins ,DPPH ,Protein Hydrolysates ,medicine.medical_treatment ,Clinical Biochemistry ,Egg protein ,Peptide ,Saccharomyces cerevisiae ,Biochemistry ,Hydrolysate ,chemistry.chemical_compound ,food ,Pepsin ,Yolk ,medicine ,Animals ,Glycoside Hydrolase Inhibitors ,IC50 ,chemistry.chemical_classification ,Chromatography ,biology ,Hydrolysis ,Organic Chemistry ,Egg Proteins ,alpha-Glucosidases ,Free Radical Scavengers ,Egg yolk protein by-product ,Angiotensin I-converting enzyme inhibitory activity ,chemistry ,Antidiabetic ,biology.protein ,Original Article ,Peptides ,Chickens - Abstract
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 reversed-phase 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.
- Published
- 2014