Chemical Characteristics and Activity of ACE Inhibitors on Fractionation of Tempeh Koro kratok (Phaseolus lunatus) Peptides

https://doi.org/10.22146/ifnp.46733

Marta Tika Handayani(1*), Retno Indrati(2), Muhammad Nur Cahyanto(3)

(1) Universitas Gadjah Mada
(2) Faculty of Agricultural Technology, Universitas Gadjah Mada
(3) Faculty of Agricultural Technology, Universitas Gadjah Mada
(*) Corresponding Author

Abstract


Tempeh is a fermented food that is good for health and has high nutritional value. Koro kratok tempeh is one of tempeh which is made from non-soybean legumes. The fermentation process will convert macromolecular compounds to micromolecules thereby increasing bioavailability and providing functional properties. This study aimed to find out the chemical properties of koro kratok tempeh and the effect of peptide molecular weight of koro kratok tempeh on ACE inhibition activity. The results show that koro kratok seeds contained 20.66% protein which total hydrophobic amino acid was 3.32% (w/w protein). This hydrophobic amino acid was higher than that soybean, indicated that koro kratok (Phaseolus lunatus) has a potential producing ACE peptide inhibitors. The koro kratok seeds had ACE inhibitory activity  19.72%. This activity increased to 84.97% when the seeds were fermented for 48h to become tempeh. Peptide fractionation showed that the smaller the molecular weight of the peptide, the higher the ACE inhibitory activity.


Keywords


Tempe; koro kratok; fractionation; ACE-inhibitor

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References

AOAC. Official Methods of Analysis of the Association of Official Analytical Chemists, 16th Een. Washington DC: AOAC (2005).

Balti R., Bougatef A., Sila A., Guillochon D., Dhulster P., Nedjar-Arroume N. (2015). Nine Novel Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Cuttle Fish (Sepia officinalis) Muscle Protein Hydrolysates and Antihypertensive Effect of the Potent Active Peptide in Spontaneously Hypertensive Rats, FoodChem. 170 : 519–525.

Baudoin JP, Rocha O, Degreef J, Maquet A, Guarino L. (2004). Ecogeography, Demography, Diversity and Conservation of Phaseolus lunatus L. In the Central Valley of Costa Rica. In: Sysematic and Ecogeographic Studies on Crop Genepools 12. International Plant Genetic Resource Institute [IPGRI], Roma, Italy.

Budi Widianarko, Rika Pratiwi, Soedarini, Rossana Dewi, Sri Wahyuningsih, danNunik Sulistiyani. (2003). Menuai Polong, Sebuah Pengalaman Advokasi Keragaman Hayati. Gramedia Widiasarana. Jakarta.

Bujang, A., and Nurul A.T. (2014). Change on Amino Acid Content in Soybean, Garbamzo Bean and Groundnut During Pre-treatment and Tempe Making. Sains Malaysiana, 43(4), 551-557.

Chel-Guerrero, L., Adriana A. S., Santiago G. T., Gloria D., and Maria C. A. (2007). Physicochemical and Structural Characterization of Ilma Bean (Phaseolus lunatus) Globulins. LWT, 40 : 1537-1544.

Cushman DW, Cheung HW. (1971). Spectrophotometric Assay and Properties of the Angiotensin Converting Enzyme of the Rabbit Lung. Biochem Pharmacol 20:1637 – 1648.

Darewicz, M., Borawska J., Vegarud G. E., Minkiewicz P., and Iwaniak A. (2014). Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity An ACE Inhibitory Peptides of Salmon (Salmo salar) Protein Hydrolysates Obtained by Human and Porcine Gastrointestinal Enzymes. International Journal of Molecular Sciences, 15, 14077–14101.

Daskaya-Dikmen, C. et al. (2017) ‘Angiotensin-I-converting enzyme (ACE)-inhibitory peptides from plants’, Nutrients, 9(4), pp. 1–19. doi: 10.3390/nu9040316.

Deddish, P.A., Wang, J., Michel, B., Morris, P.W., Davidson, N.O., Skidgel, R.A., Erdös, E.G. 1994. Naturally Occurring Active N-Domain of Human Angiotensin I-Converting Enzyme. Proc. Natl. Acad. Sci. 91, 7807–7811.

Karmini, M., Sutopo, D., dan Hermana. 1996. Aktivitas Enzim Hidrolik Kapang Rhizopus sp pada Proses Fermentasi Tempe. Penelitian Gizi dan Makanan 19:93-102.

Lee, D.H., Kim J.H., Park J.S., Choi Y.J., 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.

Lee, S. Y. and Hur, S. J. (2017) ‘Antihypertensive peptides from animal products, marine organisms, and plants’, Food Chemistry. Elsevier Ltd, 228, pp. 506–517. doi: 10.1016/j.foodchem.2017.02.039.

LuoAs I.M., Alexander B.M., Oliveira M. M., Abreu I.A. 2016. Selection of An Appropriate Protein Extraction Method to Study the Phosphoproteome of Maize Photosynthetic Tissue. PLOS ONE 11(10): e)164387.

Maesan, V. D dan Somaatmadja S. 1993. Proses Sumber Daya Nabati Asia Tenggara. Jakarta : Penerbit Gramedia Pustaka Utama.

Magana, M.D., Maira S.C., Gloroa D.O., David B.A., Luis C.G. 2015. ACE-I Inhibitory Properties of Hydrolysates from Germinated and Ungerminated Phaseoulus lunatus Proteins. Food Science and Technology 35(1): 167-174.

Malaguti, M., Dinelli, G., Leoncini, E., Bregola, V., & Bosi, S. (2014). Bioactive Peptides in Cereals and Legumes : Agronomical, Biochemical and Clinical Aspects, 21120–21135. https://doi.org/10.3390/ijms151121120.

Mechin V., Damerval C., Zivy M. 2007. Total Protein Extraction with TCA-Acetone. In: Thiellement H, Zivy M., Damerval C., Mechin V., Editors. Plant Proteomics: Methods and Protocols. Methods in Molecular Biology. 355. New Jersey: Humana Press.

Moayedi, A., Mora L., Aristoy M.C., Hashemi M. Safari M., Toldrá F. 2018. 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. Appl. Biochem. Biotechnol, 181, 48–64.

Natesh R., Schwager SL., Sturrock ED, Asharya KR. 2003. Crystal Structure of the Human Angiotensin-Converting Enzyme-Lisinopril Complex, Nature, 421 (6922): 551-4.

Nout, M.J.R., Kiers J.L. 2005. Tempe Fermentation, Innovation and Functionality: Update Into the Third Millennium. Journal of Applied Microbiology 98: 789-805.

Pan, D., Huiqing G., Bo Z., Jinxuan C. 2011. The Molecular Mechanisms of Interactions Between Bioactive Peptides and Angiotensin-Converting Enzyme. Bioorganic & Medicinal Chemistry Letter 21: 3898-3904.

Pohl, T. 1990. Concentration of Protein Removal of Salute dalam M.P. Deutscher, Methods of Enzymology: Guide to Protein Purification.Vol: 182. Academic Press. New York.

Power, O., Fernández A., Norris R., Riera F. A., and FitzGerald R. J. 2014. Selective Enrichment of Bioactive Properties during Ultrafiltration of A Tryptic Digest of β-lactoglobulin. Journal of Functional Foods, 9, 38–47.

Sornwatana, T., Bangphoomi K., Roytrakul S., Wetprasit N., Choowongkomon K., Ratanapo S. 2015. Chebulin: Terminalia Chebula Retz. Fruit-Derived Peptide with Angiotensin-I-Converting Enzyme Inhibitory Activity. Biotechnol. Appl. Biochem, 62, 746–753.

Stephanie, and Purwadaria T. 2013. Fermentasi Substrat Padat Kulit Singkong Sebagai Bahan Pakan Ternak Unggas. Wartazoa. 23:15-22.

Tamam B., Dahrul S., Hanifah N. L., Maggy T. S., and Wisnu A. K. 2018. Beberapa Penciri Berbasis Sekuens Untuk Mengenali Sifat Fungsional Peptida Bioaktif : Studi Eksplorasi. J. Teknol. Dan Industri Pangan, 29 (1), 1-9.

Tejasari. 2016. Protein Density and Quality of Koro kratok (Phaseolus lunatus L. Sweet) and Kacang Tunggak (Vurga unguiculata (L) Walp). Proceeding ICMHS. ISBN 978-602-60569-3-1.

Toopcham, T., Sittiruk R., Jirawat Y. 2015. Characterization and Identification of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides Derived from Tilapia Using Virgibacillus Halodenitrificans SK1-3-7 proteinases. Journal of Functional Foods, 14: 435 - 444.

Uco, J.T., Luis C.G., Alma M.A., Gloria D.O., David B.A., 2009. Angiotensin-I Converting Enzyme Inhibitory and Antioxidant Activities of Protein Hydrolysates from Phaseolus lunatus and Phaseolus vulgaris seeds. Food Science and Technology, 42: 1597-1604.

Wang, C., Ma, Q., Pagadala, S., Serrard, M.S., adn Krishnan, P.G. 1998. Changes of During Processing of Soybean Protein Isolates. J. Am. Oil Chem. Soc. 75: 337-341.

Wang, X., Chen H., Fu X., Li S.,Wei J. 2017. A Novel Antioxidant and ACE-Inhibitory Peptide from Rice Bran Protein: Biochemical Characterization and Molecular Docking Study. LWT-Food Sci. Technol, 75, 93–99.

White, B. L., Sanders T. H., Davis J. P. 2014. Potential ACE-Inhibitory Activity and Nano-LC-MS/MS Sequencing of Peptides Derived from Aflatoxin Contaminated Peanut Meal. LWT-Food Sci. Technol, 56, 537–542.



DOI: https://doi.org/10.22146/ifnp.46733

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Indonesian Food and Nutrition Progress (print ISSN 0854-6177, online ISSN 2597-9388) is published by the Indonesian Association of Food Technologist in collaboration with Department of Food and Agricultural Product Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada.

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