Isolation and Characterization of a Potential Angiotensin-Converting Enzyme Inhibitory Peptide from the Leaves of Leptadenia hastata (Asclepiadaceae)
Abstract
This paper describes the isolation, purification and characterization of a potential Angiotensin-Converting Enzyme (ACE) inhibitory peptide from the leaves of Leptadenia hastata (Asclepiadaceae). The leaves were collected from Kano state, Nigeria. Crude proteins were extracted from the leaves using a protein extraction kit. The proteins were purified by a three-step method: cold acetone precipitation, gel filtration using chromatography sephadex G-100 and ion exchange chromatography using CM-sephadex. The ACE inhibitory activity, protein content, effect of pH, temperature and digestive enzymes on the activity of the isolated and purified peptide were determined. In addition, the inhibition pattern, amino acid composition and sequence of the purified peptide were investigated. The specific inhibitory activity of the peptide increased from 0.0018 to 0.0085 U.mg-1 at a purification fold of 4.72 and yield of 9.57%. The optimum temperature and pH of the peptide ACE inhibitory activity was found to be 40ºC and 7.0 respectively. The digestive enzymes, pepsin and trypsin significantly (P<0.05) reduced the activity of the peptide compared to antihypertensive drug enalapril. The amino acid composition of the peptide was found to be aspartate (Asp), glutamate (Glu), glycine (Gly), valine (Val), leucine (Leu) and phenylalanine (Phe). The purified peptide showed a mixed pattern type of ACE inhibition. In conclusion, the results of this work suggest that Leptadenia hastata (Asclepiadaceae) leaves could be a potential source of peptides with high ACE inhibitory activities.
Keywords: Leptadenia hastata (Asclepiadaceae); angiotensin converting enzyme; hypertension; peptide.
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