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Production of Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptides during the Fermentation of Jack Bean (Canavalia ensiformis) Tempe
Abstract
Background and Objective: Angiotensin-converting enzyme (ACE) inhibitory peptides from various food sources have been studied extensively. We are interested in studying the inhibition of ACE from fermented tempe made from the jack bean, which is a commonly used source of plant-based protein. The purpose of this study was to determine the optimal incubation period for the production of peptides with high ACE inhibitory activity. Materials and Methods: After soaking and boiling, the jack beans were inoculated with tempe inoculum and incubated for 0-120 h. During the incubation, various parameters, such as proteolytic activity, peptide content, hydrolysis degree, protein pattern and ACE inhibition, were monitored. All the parameters were measured using standard methods. Results: Tempe fermentation caused hydrolysis of the jack bean protein, producing soluble high molecular weight proteins (from previously insoluble) and protein fragments (monitored from SDS PAGE data). The highest protein hydrolysis occurred after 96 h fermentation period, which were observed from the highest proteolytic activity (25.39 units g–1), hydrolysis degree (19.85%) and peptide content (6.05 mg mL–1). The highest ACE inhibitory activity did not coincide with the highest levels of protein hydrolysis but rather were obtained after 72 h of tempe fermentation (IC50 = 1.03 mg mL–1). Conclusion: Jack bean tempe is a potential source of ACE inhibitory peptides, the highest ACE inhibitory activity occurred after 72 h of incubation.
Keywords:
ACE, fermentation, hydrolysis, jack bean, peptides, protease, tempeArticle Metrics
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This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution and reproduction in any medium, provided the original author and source are credited.
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Puspitojati, E., Cahyanto, M. N., Marsono, Y., & Indrati, R. (2019). Production of Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptides during the Fermentation of Jack Bean (Canavalia ensiformis) Tempe. Pakistan Journal of Nutrition, 18(5), 464–470. https://doi.org/10.3923/pjn.2019.464.470
References
1.
Aluko, R.E., 2015. Antihypertensive peptides from food proteins. Annu. Rev. Food Sci. Technol., 6: 235-262.
2.
Daskaya-Dikmen, C., A. Yucetepe, F. Karbancioglu-Guler, H. Daskaya and B. Ozcelik, 2017. Angiotensin-I-Converting Enzyme (ACE)-inhibitory peptides from plants. Nutrients, Vol. 9, No. 4.
3.
Garcia, M.C., P. Puchalska, C. Esteve and M.L. Marina, 2013. Vegetable foods: A cheap source of proteins and peptides with antihypertensive, antioxidant and other less occurrence bioactivities. Talanta, 106: 328-349.
4.
Aluko, R.E., 2015. Structure and function of plant protein-derived antihypertensive peptides. Curr. Opin. Food Sci., 4: 44-50.
5.
Segura-Campos, M.R., C.P. Espadas-Alcocer, L. Chel-Guerrero and D. Betancur-Ancona, 2013. ACE-I inhibitory peptide fractions from enzymatic hydrolysates of velvet bean (Mucuna pruriens). Agric. Sci., 4: 767-773.
6.
Torruco-Uco, J., L. Chel-Guerrero, A. Martinez-Ayala, G. Davila-Ortiz and D. Betancur-Ancona, 2009. Angiotensin-I converting enzyme inhibitory and antioxidant activities of protein hydrolysates from Phaseolus lunatus and Phaseolus vulgaris seeds. Food Sci. Technol., 42: 1597-1604.
7.
Ibe, S., K. Yoshida, K. Kumada, S. Tsurushiin, T. Furusho and K. Otobe, 2009. Antihypertensive effects of natto, a traditional Japanese fermented food, in spontaneously hypertensive rats. Food Sci. Technol. Res., 15: 199-202.
8.
Gibbs, B.F., A. Zougman, R. Masse and C. Mulligan, 2004. Production and characterization of bioactive peptides from soy hydrolysate and soy-fermented food. Food Res. Int., 37: 123-131.
9.
Moayedi, A., L. Mora, M.C. Aristoy, M. Hashemi, M. Safari and F. Toldra, 2017. ACE-inhibitory and antioxidant activities of peptide fragments obtained from tomato processing by-products fermented using Bacillus subtilis: Effect of amino acid composition and peptides molecular mass distribution. Applied Biochem. Biotechnol., 181: 48-64.
10.
Wenno, M.R., E. Suprayitno, Aulanni’am and Hardoko, 2016. The physicochemical characteristics and Angiotensin Converting Enzyme (ACE) inhibitory activity of skipjack tuna (Katsuwonus pelamis) “Bakasangâ€. J. Teknol., 2: 119-124.
11.
Wikandari, P.R. and L. Yuanita, 2016. Pengaruh degradasi enzim proteolitik terhadap aktivitas angiotensin converting enzyme inhibitor bekasam dengan Lactobacillus plantarum B1765. Agritech, 36: 170-175.
12.
Shurtleff, W. and A. Aoyagi, 2011. History of Tempeh and Tempeh Products (1815-2011): Extensively Annotated Bibliography and Sourcebook. Soyinfo Center, Lafayette, Louisiana, ISBN: 9781928914396, Pages: 990.
13.
De Reu, J.C., R.M. ten Wolde, J. de Groot, M.R. Nout, F.M. Rombouts and H. Gruppen, 1995. Protein hydrolysis during soybean tempe fermentation with Rhizopus oligosporus. J. Agric. Food Chem., 43: 2235-2239.
14.
Gibbs, B.F., 2001. Production and characterization of bioactive peptides from soy fermented foods and their hydrolysates. Ph.D. Thesis, McGill University, Canada.
15.
Sukasih, E. and E.Y. Purwani, 2017. Introductory study on processing of fermented jack bean (Canavalia ensiformis). Indonesian J. Agric. Postharvest Res., 12: 129-136.
16.
Sridha, K.R. and S. Seena, 2006. Nutritional and antinutritional significance of four unconventional legumes of the genus Canavalia-A comparative study. Food Chem., 99: 267-288.
17.
Murdiati, A., S. Anggrahini, Supriyanto and A. Alim, 2015. Increased protein content of wet noodle from tapioca substituted by white jack bean (Canavalia ensiformis L.) flour. Agritech-J. Teknol. Pertanian, 35: 251-260.
18.
Suciati, A., 2012. Pengaruh lama perendaman dan fermentasi terhadap kandungan HCN pada tempe kacang koro (Canavalia ensiformis L.). Food Science Technology Department, University Hasanudin, pp: 38.
19.
Elegado, F.B. and Y. Fujio, 1993. Growth of Rhizopus strains on soybean and their protease formation. Bull. Fac. Agric. Kyushu Univ., 37: 315-324.
20.
Rusdah, 2016. Antioxidative of tempe peptides from Indonesia. Department Food Science Technology, Bogor Agricultural University, pp: 50.
21.
Cushman, D.W. and H.S. Cheung, 1971. Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochem. Pharmacol., 20: 1637-1648.
22.
Wu, Q., J. Du, J. Jia and C. Kuang, 2016. Production of ACE inhibitory peptides from sweet sorghum grain protein using alcalase: Hydrolysis kinetic, purification and molecular docking study. Food Chem., 199: 140-149.
23.
Church, F.C., H.E. Swaisgood, D.H. Porter and G.L. Catignani, 1983. Spectrophotometric assay using o-phthaldialdehyde for determination of proteolysis in milk and isolated milk proteins. J. Dairy Sci., 66: 1219-1227.
24.
Wulandari, R.D., E. Rahayu, Y. Marsono and T. Utami, 2017. [Antioxidant activity and angiotensin-I converting enzyme inhibitor of yogurt with ficus glomerata roxb leaf extract]. Agritech, 37: 246-255.
25.
Lin, H.C., A.M. Alashi, R.E. Aluko, B.S. Pan and Y.W. Chang, 2017. Antihypertensive properties of tilapia (Oreochromis spp.) frame and skin enzymatic protein hydrolysates. Food Nutr. Res., Vol. 61, No. 1.
26.
Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
27.
AOAC., 2005. AOAC Official Methods of Analysis. 15th Edn., Association of Official Analytical Chemists, Washington, D.C., pp: 136-138.
28.
Singh, B.P., S. Vij and S. Hati, 2014. Functional significance of bioactive peptides derived from soybean. Peptides, 54: 171-179.
29.
Duranti, M., 2006. Grain legume proteins and nutraceutical properties. Fitoterapia, 77: 67-82.
30.
Vadivel, V. and K. Janardhanan, 2000. Nutritional and anti-nutritional composition of velvet bean: An under-utilized food legume in South India. Int. J. Food Sci. Nutr., 51: 279-287.
31.
Oshodi, A.A. and M.O.A. Adeladun, 1993. Proximate composition, some nutritionally valuable minerals and functional properties of three varieties of Lima bean (Phaseolus lunatus Linn.) flour. Int. J. Food Sci. Nutr., 43: 181-186.
32.
Habibullah, M. Abbas and H.U. Shah, 2007. Proximate and mineral composition of mung bean. Sarhad J. Agric., 23: 463-466.
33.
Hang, M. and X.H. Zhao, 2012. Fermentation time and ethanol/water-based solvent system impacted in vitro ACE-inhibitory activity of the extract of Mao-tofu fermented by Mucor spp. CyTA-J. Food, 10: 137-143.
34.
Ni, H., L. Li, G. Liu and S.Q. Hu, 2012. Inhibition mechanism and model of an angiotensin I-converting enzyme (ACE)-inhibitory hexapeptide from yeast (Saccharomyces cerevisiae). PloS One, Vol. 7, No. 5.
35.
Sher, M.G., M. Nadeem and Q. Syed, 2011. Study on protease from barley tempeh and in vitro protein digestibility. Jordan J. Biol. Sci., 4: 257-264.
36.
Starzynska-Janiszewska, A., B. Stodolak and A. Wikiera, 2015. Proteolysis in tempeh-type products obtained with Rhizopus and Aspergillus strains from grass pea (Lathyrus sativus) seeds. Acta Sci. Pol. Technol. Aliment., 14: 125-132.
37.
Weng, T.M. and M.T. Chen, 2011. Effect of two-step fermentation by Rhizopus oligosporus and Bacillus subtilis on protein of fermented soybean. Food Sci. Technol. Res., 17: 393-400.
38.
Sturrock, E.D., R. Natesh, J.M. Van Rooyen and K.R. Acharya, 2004. Structure of angiotensin I-converting enzyme. Cell. Mol. Life Sci., 61: 2677-2686.
39.
Malaguti, M., G. Dinelli, E. Leoncini, V. Bregola, S. Bosi, A. Cicero and S. Hrelia, 2014. Bioactive peptides in cereals and legumes: Agronomical, biochemical and clinical aspects. Int. J. Mol. Sci., 15: 21120-21135.
40.
Kuba, M., K. Tanaka, S. Tawata, Y. Takeda and M. Yasuda, 2003. Angiotensin I-converting enzyme inhibitory peptides isolated from tofuyo fermented soybean food. Biosci. Biotechnol. Biochem., 67: 1278-1283.
