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 journalJournal articleResearchpeer-review

Harvard

Abdel-Hamid, M, Otte, J, De Gobba, C, Osman, A & Hamad, E 2017, 'Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins', International Dairy Journal, vol. 66, pp. 91-98. https://doi.org/10.1016/j.idairyj.2016.11.006

APA

Abdel-Hamid, M., Otte, J., De Gobba, C., Osman, A., & Hamad, E. (2017). Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins. International Dairy Journal, 66, 91-98. https://doi.org/10.1016/j.idairyj.2016.11.006

Vancouver

Abdel-Hamid M, Otte J, De Gobba C, Osman A, Hamad E. Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins. International Dairy Journal. 2017;66:91-98. https://doi.org/10.1016/j.idairyj.2016.11.006

Author

Abdel-Hamid, Mahmoud ; Otte, Jeanette ; De Gobba, Cristian ; Osman, Ali ; Hamad, Essam. / Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins. In: International Dairy Journal. 2017 ; Vol. 66. pp. 91-98.

Bibtex

@article{2fdf1c9c8dfa4443a2f9ffaf880e9b19,
title = "Angiotensin I-converting enzyme inhibitory activity and antioxidant capacity of bioactive peptides derived from enzymatic hydrolysis of buffalo milk proteins",
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",
author = "Mahmoud Abdel-Hamid and Jeanette Otte and {De Gobba}, Cristian and Ali Osman and Essam Hamad",
year = "2017",
doi = "10.1016/j.idairyj.2016.11.006",
language = "English",
volume = "66",
pages = "91--98",
journal = "International Dairy Journal",
issn = "0958-6946",
publisher = "Elsevier",

}

RIS

TY - JOUR

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