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Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins

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Authors:
  • Abdel-Hamid, Mahmoud ;
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    unknown
  • Otte, Jeanette ;
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    Orcid logo0000-0002-9444-9102
    Ingredient and Dairy Technology, Department of Food Science, Faculty of Science, Københavns Universitet
  • De Gobba, Cristian ;
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    Orcid logo0000-0002-2774-5876
    Ingredient and Dairy Technology, Department of Food Science, Faculty of Science, Københavns Universitet
  • Osman, Ali ;
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    unknown
  • Hamad, Essam
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    unknown
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

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