Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins
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Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins. / Abdel-Hamid, Mahmoud; Otte, Jeanette; De Gobba, Cristian; Osman, Ali; Hamad, Essam.
In: International Dairy Journal, Vol. 66, 2017, p. 91-98.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins
AU - Abdel-Hamid, Mahmoud
AU - Otte, Jeanette
AU - De Gobba, Cristian
AU - Osman, Ali
AU - Hamad, Essam
PY - 2017
Y1 - 2017
N2 - 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
AB - 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
U2 - 10.1016/j.idairyj.2016.11.006
DO - 10.1016/j.idairyj.2016.11.006
M3 - Journal article
VL - 66
SP - 91
EP - 98
JO - International Dairy Journal
JF - International Dairy Journal
SN - 0958-6946
ER -
ID: 176373162