STUDY ON THE AMINO ACID COMPOSITION OF CRUDE FICIN ENZYME FROM Ficus padana Burm.f. USING SOLAR DRYING
Keywords:
Ficin enzyme, Ficus padana Burm.f., Solar Drying, Crude Enzyme, Amino Acid ProfileAbstract
Ficin is an enzyme derived from Ficus sp., recognized for its applications in the food and pharmaceutical sectors. Utilizing solar energy for enzyme drying has been shown to be economical and environmentally sustainable while preserving enzyme activity. This study aimed to determine the amino acid composition of crude ficin from Ficus padana Burm. f., and was extracted and dried with solar energy. The analysis of amino acid components was conducted using the UPLC technique. The results indicated the presence of numerous important amino acids, with L-aspartic acid being the highest concentrated at 1.85 mg/g and L-leucine at 1.41 mg/g. Significant quantities of L-glutamic acid (1.33 mg/g), L-serine (1.14 mg/g), and L-lysine (1.05 mg/g) were also identified. The solar drying process showed no significant loss of amino acids. The findings suggest that solar drying does not negatively impact the amino acid composition in fiction, therefore enhancing its practical significance, particularly for the food and pharmaceutical sectors.
References
Aïder, M. (2021). Potential Applications of Ficin in the Production of Traditional Cheeses and Protein Hydrolysates. JDS Communications, 2(5), 233–237. https://doi.org/10.3168/jdsc.2020-0073
Anab-Atulomah, C., & Nwachukwu, E. (2021). Optimization of Pectinase and Protease Produced From Bacillus Subtilis Isolated From Market Waste. South Asian Journal of Research in Microbiology, 48–57. https://doi.org/10.9734/sajrm/2020/v8i330196
Babar, O. A., Tarafdar, A., Malakar, S., Arora, V. K., & Nema, P. K. (2020). Design and Performance Evaluation of a Passive Flat Plate Collector Solar Dryer for Agricultural Products. Journal of Food Process Engineering, 43(10). https://doi.org/10.1111/jfpe.13484
Boateng, I. D. (2023). A Review of Solar and Solar?assisted Drying of Fresh Produce: State of the Art, Drying Kinetics, and Product Qualities. Journal of the Science of Food and Agriculture, 103(13), 6137–6149. https://doi.org/10.1002/jsfa.12660
Boo, H.-O., Shin, J.-H., Kim, Y. S., Park, H.-J., Kim, H.-H., Kwon, S.-J., & Woo, S. H. (2013). Comparative Antioxidant Enzyme Activity of Diploid and Tetraploid Platycodon Grandiflorum by Different Drying Methods. Korean Journal of Plant Resources, 26(3), 389–396. https://doi.org/10.7732/kjpr.2013.26.3.389
Costa-Silva, T. A., Souza, C. R. F., Said, S., & Oliveira, W. P. de. (2015). Drying of Enzyme Immobilized on Eco-Friendly Supports. African Journal of Biotechnology, 14(44), 3019–3026. https://doi.org/10.5897/ajb2015.14830
Destryana, R. A., Fajarianingtyas, D. A., Wibisono, A., Witono, Y., Belgis, M., & Taruna, I. (2023). Purification of Protease Enzymes From Wild Poinsettia (Euphorbia Heterophylla) Plant With Ammonium Sulphate. Proceedings of the 2022 Brawijaya International Conference (BIC 2022). Advances in Economics, Business and Management Research., 449–456. https://doi.org/10.2991/978-94-6463-140-1_45
Gagaoua, M., Boucherba, N., Bouanane-Darenfed, A., Ziane, F., Nait-Rabah, S., Hafid, K., & Boudechicha, H. R. (2014). Three-phase partitioning as an efficient method for the purification and recovery of ficin from Mediterranean fig (Ficus carica L.) latex. Separation and Purification Technology, 132. https://doi.org/10.1016/j.seppur.2014.05.050
Hansen, B. K., Gupta, R., Baldus, L., Lyon, D., Narita, T., Lammers, M., … Weinert, B. T. (2019). Analysis of Human Acetylation Stoichiometry Defines Mechanistic Constraints on Protein Regulation. Nature Communications, 10(1). https://doi.org/10.1038/s41467-019-09024-0
Hay, S., Johannissen, L. O., Hothi, P., Sutcliffe, M. J., & Scrutton, N. S. (2012). Pressure Effects on Enzyme-Catalyzed Quantum Tunneling Events Arise From Protein-Specific Structural and Dynamic Changes. Journal of the American Chemical Society, 134(23), 9749–9754. https://doi.org/10.1021/ja3024115
Mongkolpathumrat, P., Nernpermpisooth, N., Kijtawornrat, A., Pikwong, F., Chouyratchakarn, W., Yodsheewan, R., … Kumphune, S. (2022). Adeno-Associated Virus 9 Vector-Mediated Cardiac-Selective Expression of Human Secretory Leukocyte Protease Inhibitor Attenuates Myocardial Ischemia/Reperfusion Injury. Frontiers in Cardiovascular Medicine, 9. https://doi.org/10.3389/fcvm.2022.976083
Mousavi Maleki, M. S., Aghamirza Moghim Ali Abadi, H., Vaziri, B., Shabani, A. A., Ghavami, G., Madanchi, H., & Sardari, S. (2023). Bromelain and Ficin Proteolytic Effects on Gliadin Cytotoxicity and Expression of Genes Involved in Cell-Tight Junctions in Caco-2 Cells. Amino Acids, 55(11), 1601–1619. https://doi.org/10.1007/s00726-023-03333-x
Toouli, J., Biankin, A. V, Oliver, M., Pearce, C. B., Wilson, J. S., & Wray, N. (2010). Management of Pancreatic Exocrine Insufficiency: Australasian Pancreatic Club Recommendations. The Medical Journal of Australia, 193(8), 461–467. https://doi.org/10.5694/j.1326-5377.2010.tb04000.x
Wagner, G. R., Bhatt, D. P., O’Connell, T. M., Thompson, J. W., Dubois, L. G., Backos, D. S., … Hirschey, M. D. (2017). A Class of Reactive Acyl-CoA Species Reveals the Non-Enzymatic Origins of Protein Acylation. Cell Metabolism, 25(4), 823-837.e8. https://doi.org/10.1016/j.cmet.2017.03.006
Wei, M., Chen, P., Zheng, P., Tao, X., Xiang, Y., & Wu, D. (2023). Purification and Characterization of Aspartic Protease From Aspergillus Niger and Its Efficient Hydrolysis Applications in Soy Protein Degradation. Microbial Cell Factories, 22(1). https://doi.org/10.1186/s12934-023-02047-9
Yayehrad, A. T. (2023). Physicochemical Characterization and Evaluation of Ficus Vasta Gum as a Binder in Tablet Formulation. Biomed Research International, 2023(1). https://doi.org/10.1155/2023/8852784
Goncharova, S. S., Lavlinskaya, M. S., Holyavka, M. G., Faizullin, D. A., Zuev, Y. F., … Artyukhov, V. G. (2023). Complexation of Bromelain, Ficin, and Papain With the Graft Copolymer of Carboxymethyl Cellulose Sodium Salt and N-Vinylimidazole Enhances Enzyme Proteolytic Activity. International Journal of Molecular Sciences, 24(14), 11246. https://doi.org/10.3390/ijms241411246
