期刊
AMINO ACIDS
卷 47, 期 2, 页码 369-380出版社
SPRINGER WIEN
DOI: 10.1007/s00726-014-1869-x
关键词
Egg yolk protein by-product; Hydrolysis; Antioxidant; Antidiabetic; Angiotensin I-converting enzyme inhibitory activity
资金
- European Union through the European Regional Development Fund [1.3.1]
- Wroclaw Centre of Biotechnology, programme The Leading National Research Centre (KNOW)
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 (alpha-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 A mu g/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 A mu g/mL. The peptide VTGRFAGHPAAQ revealed the highest alpha-glucosidase inhibitory activity (IC50 = 365.4 A mu g/mL). A novel nutraceutical effect for peptides from an egg yolk hydrolysate was shown.
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