Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins
- Authors:
-
- Abdel-Hamid, Mahmoud ;
-
Otte, Jeanette
;
Close
0000-0002-9444-9102
Ingredient and Dairy Technology, Department of Food Science, Faculty of Science, Københavns Universitet -
De Gobba, Cristian
;
Close0000-0002-2774-5876
Ingredient and Dairy Technology, Department of Food Science, Faculty of Science, Københavns Universitet - Osman, Ali ;
- Hamad, Essam
- DOI:
- 10.1016/j.idairyj.2016.11.006
- Abstract:
- Buffaloes' milk, which is consumed in many parts of the world, is a little-explored source of bioactive peptides. The angiotensin converting enzyme (ACE)-inhibitory activity and the antioxidant capacity of peptides from buffaloes' milk were examined. A retentate from buffaloes' skimmed milk was hydrolysed using papain, pepsin or trypsin. The papain hydrolysate showed the highest ACE-inhibitory activity and radical scavenging capacity and was fractionated by size exclusion chromatography (SEC) and characterized by LC-MS analysis. A SEC-fraction with intermediate peptide size showed very high ACE-inhibitory activity, while two fractions with small peptides exhibited the strongest antioxidant activity. Peptide identification by ultra-performance liquid-chromatography-tandem mass spectrometry showed that these active fractions contained known bioactive sequences, in addition to novel peptides with supposed ACE-inhibitory (FPGPIPK, IPPK, IVPN, and QPPQ) and antioxidant (YPSG, HPFA and KFQ) activities. The results obtained showed the potential of buffaloes' milk proteins to release ACE-inhibitory and antioxidant peptides
- Type:
- Journal article
- Language:
- English
- Published in:
- International Dairy Journal, 2017, Vol 66, p. 91-98
- Main Research Area:
- Science/technology
- Publication Status:
- Published
- Review type:
- Peer Review
- Submission year:
- 2017
- Scientific Level:
- Scientific
- ID:
- 2349079808
