Isolation and purification of angiotensin converting enzyme inhibitory peptide from goat milk hydrolysate by ultrafiltration membrane
1 Department of Biological Sciences, Federal University of Kashere, Gombe, Nigeria.
2 Centre for Biotechnology, Bayero University Kano, Kano, Nigeria.
3 Department of Biochemistry, Osun State University, Osun, Nigeria.
4 Integrated Science Department, Federal College of Education, Kano, Nigeria.
Research Article
World Journal of Advanced Research and Reviews, 2024, 22(03), 472–479
Article DOI: 10.30574/wjarr.2024.22.3.1718
Publication history:
Received on 25 April 2024; revised on 05 June 2024; accepted on 07 June 2024
Abstract:
Hypertension been a significant risk factor for cardiovascular illness. Synthesized angiotensin converting enzyme (ACE) inhibitors are active antihypertensive medicines they frequently generate unwanted side effects. This study describes the isolation and purification of an ACE inhibitory peptide from goat milk hydrolysate (Sahel breed). Hydrolysates containing angiotensin converting enzyme (ACE) inhibitory peptide were produced from goat milk by pepsin and trypsin. The strongest ACE inhibitory action was found in pepsin hydrolysate (57%) at 12h, hence was further purified. Purification was done using a 10 kDa ultrafiltration membrane and three steps of RP-HPLC to obtain ACE inhibitory peptide with activity of 84% and IC50 of 3.25±0.11 μg/ml. Lineweaver–Burks’ plots showed that the inhibitory kinetic mechanism of this peptide was competitive. In conclusion, ACE inhibitory peptide from goat milk hydrolysate treated with pepsin may be positive constituent to serve as drug against hypertension.
Keywords:
Hypertension; ACE Inhibitory Peptide; Goat Milk Hydrolysate; Purification.
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