Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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
Originalsprog | Engelsk |
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Tidsskrift | International Dairy Journal |
Vol/bind | 66 |
Sider (fra-til) | 91-98 |
Antal sider | 8 |
ISSN | 0958-6946 |
DOI | |
Status | Udgivet - 2017 |
ID: 176373162