Loading...
Identification of bioactive peptides from a papain hydrolysate of bovine serum albumin and assessment of an antihypertensive effect in spontaneously hypertensive rats
Citations
Altmetric:
Date
2016-03-31
Collections
Files
Loading...
main article
Adobe PDF, 873.06 KB
Research Projects
Organizational Units
Journal Issue
Citation
Tomas Lafarga, Rotimi E. Aluko, Dilip K. Rai, Paula O'Connor, Maria Hayes, Identification of bioactive peptides from a papain hydrolysate of bovine serum albumin and assessment of an antihypertensive effect in spontaneously hypertensive rats, Food Research International, Volume 81, 2016, Pages 91-99, ISSN 0963-9969, https://doi.org/10.1016/j.foodres.2016.01.007.
Abstract
Inhibition of angiotensin-I-converting enzyme (ACE-I), renin, and dipeptidyl peptidase-IV (DPP-IV) plays a key role in the treatment of hypertension and type-2 diabetes. The aim of this study was to isolate and characterize novel ACE-I, renin, and DPP-IV inhibitory peptides from a papain hydrolysate of bovine serum albumin (BSA). BSA was obtained from whole bovine blood and hydrolyzed with the food-grade enzyme papain. The generated hydrolysate was further purified using ultrafiltration and high performance liquid chromatography (HPLC), and a number of novel bioactive peptides were identified using de novo peptide sequencing. These included SLR, YY, ER, and FR which inhibited the activity of the enzyme ACE-I by half at a concentration of 0.17±0.02, 0.18±0.04, 0.27±0.01, and 0.42±0.02mM, respectively. In addition, the 1kDa fraction of the papain hydrolysate was assessed for antihypertensive activity in vivo using spontaneously hypertensive rats (SHRs) and reduced systolic blood pressure over a 24h period when compared with the control (p<0.001). Results demonstrated the potential of bovine serum albumin as a source of bioactive peptides with health-promoting properties and potential for use as functional food ingredients.