Angiotensin Converting Enzyme (ACE) Inhibitory Activity of Peptide Fraction of Germinated Pigeon Pea (Cajanus cajan (L.) Millsp.)

https://doi.org/10.22146/ijc.37513

Ketut Ratnayani(1*), I Ketut Suter(2), Nyoman Semadi Antara(3), I Nengah Kencana Putra(4)

(1) Department of Chemistry, Faculty of Natural Sciences, Udayana University, Denpasar 80361, Indonesia
(2) Department of Food Science and Technology, Faculty of Agricultural Technology, Udayana University, Denpasar 80361, Indonesia
(3) Department of Agroindustrial Technology, Faculty of Agricultural Technology, Udayana University, Denpasar 80361, Indonesia
(4) Department of Food Science and Technology, Faculty of Agricultural Technology, Udayana University, Denpasar 80361, Indonesia
(*) Corresponding Author

Abstract


During the germination process, seeds can release various types of peptides due to the degradation of storage proteins. Some of these peptides can have biological activity (bioactive peptides). The objective of this study was to determine the ACE inhibitory activity of germinated pigeon pea peptide extract at various germination times and to carry out the fractionation to the extract to get the most active peptide fraction. The results showed that the highest activity of peptide extract was found on the 4th-day germination of pigeon pea with an IC50 value of 63.46 μg/mL. The peptide extract was further fractionated by centrifugal ultrafiltration method and it was found that the peptide fraction < 3 kDa had the highest ACE inhibitory activity with an IC50 value of 57.79 μg/mL. The result of identification with the LCMS method to the fraction was able to detect 4 types of the peptide with a molecular weight of 230.304, 294.303, 441.436, and 570.591 Da. These results suggested that the peptide fraction of germinated pigeon pea has the potency as an ACE inhibitory nutraceutical.

Keywords


pigeon pea; peptide fraction; ACE inhibitory; germination

Full Text:

Full Text PDF


References

[1] de Castro, R.J.S., and Sato, H.H., 2015, Biologically active peptides: Processes for their generation, purification and identification, and applications as natural additives in the food and pharmaceutical industries, Food Res. Int., 74, 185–198.

[2] Malaguti, M., Dinelli, G., Leoncini, E., Bregola, V., Bosi, S., Cicero, A.F.G., and Hrelia, S., 2014, Bioactive peptides in cereals and legumes: Agronomical, biochemical and clinical aspects, Int. J. Mol. Sci., 15, 21120–21135.

[3] Sangronis, E., and Machado, C.J., 2007, Influence of germination on the nutritional quality of Phaseolus vulgaris and Cajanus cajan, LWT Food Sci. Technol., 40 (1), 116–120.

[4] Sefatie, R.S., Fatoumata, T., Eric, K., Shi, Y.H., and Le, G., 2013, In vitro antioxidant activities of protein hydrolysate from germinated black soybean (Glycine max L.), Adv. J. Food Sci. Technol., 5(4), 453–459.

[5] Singh, U., and Jambunathan, R., 1982, Distribution of seed protein fractions and amino acids in different anatomical parts of chickpea (Cicer arietinum L.) and pigeon pea (Cajanus cajan L.), Plant Foods Hum. Nutr., 31 (4), 347–354.

[6] Mandal, P., Misra, T.K., Sarkar, A., Ghosh, A., and Sircar, P.K., 2008, Dynamic peptide profiles of germinating mungbean: In relation to their nature and separation pattern, Indian J. Plant Physiol., 13 (2), 111–117.

[7] Bamdad, F., Dokhani, S., Keramat, J., and Zareie, R., 2009, The impact of germination and in vitro digestion on the formation of Angiotensin Converting Enzyme (ACE) inhibitory peptides from lentil proteins compared to whey proteins, Int. J. Nutr. Food Eng., 3 (1), 109–119.

[8] Layne, E., 1957, Spectrophotometric and turbidimetric methods for measuring proteins, Methods Enzymol., 3, 447–455.

[9] Cushman, D.W., and Cheung, H.S., 1971, Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung, Biochem. Pharmacol., 20 (7), 1637–1648.

[10] Siow, H.L., and Gan, C.Y., 2013, Extraction of antioxidative and antihypertensive bioactive peptide from Parkia speciosa seeds, Food Chem., 141 (4), 3435–3442.

[11] Waters, 1993, ACCQ-Fluor Reagent Kit, http://www.waters.com/webassets/cms/support/docs/wat0052881.pdf.

[12] Waters, 2005, Masslynx 4.1. Getting Starting Guide, Waters Corporation, USA.

[13] Xiao, J.F., Zhou, B., and Ressom, H.W., 2012, Metabolite identification and quantitation in LC-MS/MS-based metabolomics, Trends Anal. Chem., 32, 1–14.

[14] Sangronis, E., Rodriguez, M., Cava, R., and Torres, A., 2006, Protein quality of germinating Phaseolus vulgaris, Eur. Food Res. Technol., 222 (1-2), 144-148.

[15] Chinq-Mars, C.D., 2006, Angiotensin converting enzyme inhibitory peptide from the hydrolysis of Pacific Hake fillet by commercial protease, Thesis, British Columbia University.

[16] Ryan, J.T., Ross, R.P., Bolton, D., Fitzgerald, G.F., Stanton, C., 2011, Bioactive peptide from muscle sources: Meat and fish, Nutrients, 3 (9), 765–791.

[17] Natesh, R., Schwager, S.I.U., Sturrock, E.D., and Achraya, K.R., 2003, Crystal structure of the human angiotensin-converting enzyme-lisinopril complex, Nature, 421 (6922), 551–554.

[18] Cheung, H.S., Wang, F.L., Ondetti, M.A., Sabo, E.F., and Cushman, D.W., 1980, Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence, J. Biol. Chem., 255 (2), 401-407.



DOI: https://doi.org/10.22146/ijc.37513

Article Metrics

Abstract views : 436 | views : 396


Copyright (c) 2019 Indonesian Journal of Chemistry

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

 


Indonesian Journal of Chemisty (ISSN 1411-9420 / 2460-1578) - Chemistry Department, Universitas Gadjah Mada, Indonesia.

Web
Analytics View The Statistics of Indones. J. Chem.