Isolation and Characterization of a Potential Angiotensin-Converting Enzyme Inhibitory Peptide from the Leaves of Leptadenia hastata (Asclepiadaceae)

Mansurah Abdulazeez, Salisu Maiwada Abubakar, Sa’id Ibrahim, Jafar Musa Mu’azzam


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 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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Abdulazeez, M.A., Fatope Y., Gwani, H., Abdulazeez A. and Sadiq, F. Z. (2013). Hypolipidemic and angiotensin converting enzyme inhibitory effect of Peristrophebi calyculata (Retz.) Nees. Am. J. Biochem. Mol. Biol. 3 (2): 228-239.

Abdulazeez, M.A., Ndubuisi, T. C., Mohammed I., Abdullahi, S. A., Chintem, W. and A.M. Wudil (2015a). Partial-purification and characterization of Angiotensin Converting Enzyme inhibitory proteins from the leaves and seeds of Moringa oleifera. Int. J. Biochem. Res. Rev.5(1): 39-48.

Abdulazeez, A.M, Ibrahim, S., Ayo, J. O, Luiz, J.C.B. Carvalho, Jiradej, M. and Ibrahim , A. B. (2015b). Bioassay-guided fractionation and antihypertensive properties of fractions and crude extracts of Peristrophebi calyculata (Retz) Nees. Acta Pol. Pharm.72(2): 319-328.

Abdulazeez, A.M., Ajiboye, O.S., Wudil, A.M. and H. Abubakar (2016). Partial purification and characterization of angiotensin converting enzyme inhibitory alkaloids from the leaves and seeds of Moringa oleifera. J. Adv. Biotech. 5(2): 1-11

Aliero, A.A. and S.H. Wara (2009). Validating the medicinal potential of Leptadenia hastata. Afr. J. Pharm. Pharmacol. 3: 335-338.

Aliero, B.L., Umar, M.A., Suberu, H.A. and Abubakar, A. (2001). A Hand Book of Common Plant in North Western Nigeria. Usmanu Danfodio University Press, Sokoto, Nigeria. 78p.

Aprilita, R., Maksum, R., Abdul, M. and Suyatna, F.D. (2013). Screening Angiotensin Converting Enzyme (ACE) Inhibitor Activity of Antihypertensive Medicinal Plants from Indonesia. Int. J. Pharm. Teach. Pract. 4(1): 527-532.

Arbonnier, M. (2000). Trees, shrubs and vines dry areas of West Africa. Mali, Ouagadougou Centre for International Cooperation in Agronomic Research for Development/National Museum of Natural History/World Conservation Union (CIRAD / MNHN / IUCN). 541 p.

Bako, S.P., Bakfur, M.J., John, I. and Bala, E.I. (2005). Ethnomedicinal and Phytochemical profile of some savanna plant species in Nigeria. Int. J. Bot.1 (2): 147-150.

Barbana, C. and Boye J.I. (2011). Angiotensin I-converting enzyme inhibitory properties of lentil protein hydrolysates: Determination of the kinetics of inhibition. Food Chem. 127: 94-101.

Burkill, H.M. (1985). The useful plants of West Tropical Africa. 2nd Edition. Royal Botanic Gardens, Kew, United Kingdom. 1: 960p.

Benitez, L.V. (1989). Amino acid and fatty acid profiles in aquaculture nutrition studies. In S. S. De Silva (ed.) Pp.23-35.

Chia-Ling J., Shih-Li H. and Kuo-Chiang, H. (2012). Angiotensin I-converting enzyme inhibitory peptides: Inhibition mode, bioavailability, and antihypertensive effects. Biomed.2: 130-136.

Choi, H.S., H.Y. Cho, H.C. Yang, K.S. Ra and Suh, H.J (2001). Angiotensin I-converting enzyme inhibitor from Grifola frondosa. Food Res. Int.34: 177-182.

Dambatta, S.H. and Aliyu, B.S. (2011). A survey of major ethnomedicinal plants of Kano North Nigeria, their knowledge and uses by traditional healers. BAJOPAS.4: 28-34.

Fujita, H. and M. Yoshikawa (1999). LKPNM: A prodrug-type ACE-inhibitory peptide derived from fish protein. Immunopharmacology. 44: 123-127.

Fujita, H., Yokoyama, K. and Yoshikawa, M. (2000). Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food protein. J. Food Sci. 65: 564–569.

Ibrahim, H.A., Ali, G.Y., Halliru, S.N., Usaini, S. and Abdullahi, I.I. (2012). Ethnobotanical Survey of the Wild Edible Food Plants Consumption among Local Communities in Kano State, North Western, Nigeria. IJST. 2: 713-717.

Jang, J.H., Jeong, S.C., Kim, J.H., Lee, Y.H., Ju, Y.C. and Lee, J.S. (2011). Characterization of a new antihypertensive angiotensin I-converting enzyme inhibitory peptide from Pleurotus cornucopiae. Food Chem. 127, 412–418.

Jiapei, W., Jianen, H. and Jinzhe, C. (2008). Purification and identification of a ACE inhibitory peptide from oyster proteins hydrolysate and the antihypertensive effect of hydrolysate in spontaneously hypertensive rats. Food Chem. 111(2): 302-308.

Jung, W.K., Mendis, E., Je, J.Y., Park, P.J., Son, B.W. and Kim, H.C. (2006). Angiotensin I-converting enzyme inhibitory peptide from yellowfin sole (Limanda aspera) frame protein and its antihypertensive effect in spontaneously hypertensive rats. Food Chem. 94: 26-32.

Kerarho, J. and Adam, J.G. (1974). The traditional Senegalese pharmacopoeia: Medicinal and poisonous plants. Vigot Brother’s ed. Paris. 102p.

Koo, S.H., Ho, W.F. and Lee, E.J. (2006). Genetic polymorphisms in KCNQ1, HERG, KCNE1 and KCNE2 genes in the Chinese, Malay and Indian populations of Singapore. Br. J. Clin. Pharmacol. 61(3):301-8.

Kuba, M., Tanaka, K., Tawata, S., Takeda, Y. and M. Yasuda (2003). Angiotensin I converting enzyme inhibitory peptides isolated from fermented soybean food. Biosci. Biotechnol. Biochem. 67: 1278-1283.

Li, G.H., Le, G.W., Shi, Y.H. and Shrestha S. (2004). Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutr. Res. 24: 469-486.

Lee D.H., Kim J.H., Park, J.S., Choi, Y.J. and Lee, J.S. (2004). Isolation and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from the edible mushroom Tricholoma giganteum. Peptides.25: 621-627.

Matsui, T., Li, C.H., Tanaka, T., Maki, T., Osajima, Y. and K. Matsumoto. (2000). Depressor effect of wheat germ hydrolysate and its novel angiotensin I-converting enzyme inhibitory peptide, Ile-Val-Tyr, and the metabolism in rat and human plasma. Biol. Pharm. Bull.23: 427-431.

Min-Suk M., Bae, I.Y., Gyu, H.L. and C. Yang (2006). Purification and identification of angiotensin I-converting enzyme inhibitory peptide from buckwheat (Fagopyrum esculentum Moench). Food Chem. 96: 36-42

Nakagomi, K., Ebisu, H., Sadakane, Y., Fujii, N., Akizawa, T. and T. Tanimura. (2000). Properties and human origin of two angiotensin I-converting enzyme inhibitory peptides isolated from a tryptichydrolysate of human serum albumin. Biol. Pharm. Bull. 23: 879-883.

Ondetti, M.A. and D.W. Cushman (1982). Enzymes of the renin angiotensin system and their inhibitors. Ann. Rev. Biochem.51: 283-308.

Qu, W. Haile, M., Zhongli, P., Lin, L., Zhenbin, W. and H. Ronghai. (2010). Preparation and antihypertensive activity of peptides from Porphyrayezoensis. Food Chem. 12: 14-20.

Reddy, S.K. and M.B. Katan. (2004). Diet, nutrition and the prevention of hypertension and cardiovascular diseases. Public Health Nutr. 7(1A): 167-186.

Sallau, A.B., Ibrahim, M.A., Salihu, A. and F.U. Patrick. (2008). Characterization of phospholipase A2 (PLA2) from Echisocellatus venom. Afr. J. Biochem Res. 2(4): 98-101.

Sheih, L.C., Tony, J.F. and W. Tung-Kung. (2009). Isolation and characterization of a novel angiotensin I-converting enzyme (ACE) inhibitory peptide from the algae protein waste. Food Chem. 115: 279–284.

Tamboura, H.H‚ Bayala, B., Lompo, M., Guissou, I.P. and L. Sawadogo. (2005). Ecological distribution, morphological characteristics and acute toxicity of aqueous extracts of Holarrhena floribunda (G. Don) Durand & Schinz, Leptadenia hastate (Pers.) Decne and Cassia sieberiana (dc) used by veterinary healers in Burkina Faso. Afr. J. Tradit. Complement. Altern. Med. 2: 13-24.

Vercruysse, L. and J.V.C. Smagghe. (2005). ACE Inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein: A Review. J. Agric. Food Chem. 53: 8106-8115.

Wilson, J., Hayes, M. and B. Carney. (2011). Angiotensin-I-converting enzyme and prolyl endopeptidase inhibitory peptides from natural sources with a focus on marine processing by-products. Food Chem. 129: 235-244.


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