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Comparative Studies on the Properties of Peroxidase Partially Purified from Different Parts of Carica papaya
Current Issue
Volume 3, 2018
Issue 4 (August)
Pages: 41-46   |   Vol. 3, No. 4, August 2018   |   Follow on         
Paper in PDF Downloads: 28   Since Oct. 26, 2018 Views: 1235   Since Oct. 26, 2018
Roy Emochone Yohanna, Department of Biochemistry, Federal University Wukari, Wukari, Nigeria.
Mida Habila Mayel, Department of Biochemistry, Federal University Wukari, Wukari, Nigeria.
Richard-Harris Nsenreuti Boyi, Department of Biochemistry, Federal University Wukari, Wukari, Nigeria.
Sabinus Oscar Onyebuchi Eze, Department of Biochemistry, University of Nigeria, Nsukka, Nigeria.
Peroxidase (E.C. is an enzyme with wide industrial and biotechnological applications. However, the high cost of commercially available peroxidase places a barrier to its utilization in so many places in the world. Carica papaya Linn. (Pawpaw) has been known as a good source of peroxidase. This study was aimed at identifying the part of papaya with the highest concentration of peroxidase. Peroxidase was extracted from different parts (fruit, leaf and stem) of papaya plant and partially purified through ammonium sulphate precipitation. Peroxidase activity was measured as the change in absorbance due to the oxidation of O-dianisidine in the presence of H2O2. The Vmax and Km were determined from Lineweaver-Burk plot. Highest peroxidase activity was observed after ammonium sulphate precipitation at 60%, 50% and 70% for the fruit, leaf and stem, respectively. The pH and temperature optima for peroxidase were found to depend on the part of the plant: fruit (pH 6.5, 60°C), leaf (pH 7.0, 40°C) and stem (pH 5.5, 70°C). Peroxidase activity in the leaf (38.4 U/ml) was found to be higher than in the stem (8.6 U/ml) and the unripe Carica papaya fruit (0.74 U/ml). From the Lineweaver-Burk plot, peroxidase from the fruit had larger Vmax and Km values (Vmax = 0.678 µmol/min, Km = 0.63 µmol/min) than both from the leaf (Vmax = 0.77 µmol/min, Km = 0.57 µmol/min) and the stem (Vmax = 0.608 µmol/min, Km = 0.171). Hence, the leaf of Carica papaya can serve as cheap source of peroxidase for industrial application.
Enzyme Activity, Biotechnology, Peroxidase, Bioremediation, Lipid Peroxidation, Catalysts
Zia, M. A., Kousar, M., Ahmed, I., Igbal, H. M. N. and Abbas, R. Z. (2011). Comparative study of peroxidase purification from apple and orange seeds. African Journal of Biotechnology, 10 (33), 6300–6303.
Passardi, F., Longet, D., Penel, C., and Dunand, C. (2004). The class III peroxidase multigenic family in rice and its evolution in land plants. Phytochemistry, 65 (13), 1879–1893.
Pandey, V. P., Awasthi, M., Singh, S., Tiwari, S., and Dwivedi, U. N. (2017). A Comprehensive review on function and application of Plant peroxidases. Biochemistry and Analytical Biochemistry, 06 (01), 1–16.
Falade, A. O., Nwodo, U. U., Iweriebor, B. C., Green, E., Mabinya, L. V., and Okoh, A. I. (2017). Lignin peroxidase functionalities and prospective applications. Microbiology Open, 6 (1), 1–14.
Osuji, A. C., Eze, S. O. O., Osayi, E. E., and Chilaka, F. C. (2014). Biobleaching of industrial important dyes with peroxidase partially purified from garlic. Scientific World Journal, 2014.
Siddiqui, K. S., Ertan, H., Charlton, T., Poljak, A., Daud Khaled, A. K., Yang, X., and Cavicchioli, R. (2014). Versatile peroxidase degradation of humic substances: Use of isothermal titration calorimetry to assess kinetics, and applications to industrial wastes. Journal of Biotechnology, 178 (1), 1–11.
Bilal, M., and Asgher, M. (2015). Dye decolorization and detoxification potential of Ca-alginate beads immobilized manganese peroxidase. BMC Biotechnology, 15 (1), 1–14.
Qiao, F., Qi, Q., Wang, Z., Xu, K., and Ai, S. (2016). MnSe-loaded g-C3N4 nanocomposite with synergistic peroxidase-like catalysis: Synthesis and application toward colorimetric biosensing of H2O2 and glucose. Sensors and Actuators, B: Chemical, 229, 379–386.
Wang, S., Wang, Q., Fan, X., Xu, J., Zhang, Y., Yuan, J., and Cavaco-Paulo, A. (2016). Synthesis and characterization of starch-poly (methyl acrylate) graft copolymers using horseradish peroxidase. Carbohydrate Polymers, 136, 1010–1016.
Tian, J., Liu, Q., Asiri, A. M., Qusti, A. H., Al-Youbi, A. O., and Sun, X. (2013). Ultrathin graphitic carbon nitride nanosheets: A novel peroxidase mimetic, Fe doping-mediated catalytic performance enhancement and application to rapid, highly sensitive optical detection of glucose. Nanoscale, 5 (23), 11604–11609.
Chen, L. C., Chung, Y. C., and Chang, C. T. (2012). Characterisation of an acidic peroxidase from papaya (Carica papaya L. cv Tainung No. 2) latex and its application in the determination of micromolar hydrogen peroxide in milk. Food Chemistry, 135 (4), 2529–2535.
Eze, S. O. O. (2013). Kinetic analysis of the thermostability of peroxidase from African oil bean (Pentaclethra macrophylla Benth) seeds. Journal of Biochemical Technology, 4 (1), 459–463.
Zámocký, M., Hofbauer, S., Schaffner, I., Gasselhuber, B., Nicolussi, A., Soudi, M., and Obinger, C. (2015). Independent evolution of four heme peroxidase superfamilies. Archives of Biochemistry and Biophysics, 574, 108–119.
Kajla, M., Biol, J. P. E., Kajla, M., Gupta, K., Kakani, P., Dhawan, R., and Gakhar, S. K. (2016). Identification of an Anopheles lineage-specific unique heme peroxidase HPX15: a plausible candidate for arresting malaria parasite development. Journal of Phylogenetics and EvolutionaryBiology. 3 (4), 1-10.
Pey, A., Zamoum, T., Christen, R., Merle, P. L., and Furla, P. (2017). Characterization of glutathione peroxidase diversity in the symbiotic sea anemone Anemonia viridis. Biochimie, 132 (2017), 94–101.
Singh, H., Dixit, S., Verma, P. C., and Singh, P. K. (2013). Differential peroxidase activities in three different crops upon insect feeding. Plant Signaling and Behavior, 8 (9), 1–7.
Nnamchi, C. I., Parkin, G., Efimov, I., Basran, J., Kwon, H., Svistunenko, D. A., and Raven, E. L. (2016). Structural and spectroscopic characterisation of a heme peroxidase from sorghum Topical Issue in Honor of R. J. P. Williams. Journal of Biological Inorganic Chemistry, 21 (1), 63–70.
Yogiraj, V., Goyal, P. K., Chauhan, C. S., Goyal, A., and Vyas, B. (2014). Carica papaya Linn: an overview. International Journal of Herbal Medicine, 2 (5 Part A), 1–8.
Pandey, V. P., Singh, S., Singh, R., and Dwivedi, U. N. (2012). Purification and characterization of peroxidase from papaya (Carica papaya) fruit. Applied Biochemistry and Biotechnology, 167 (2), 367–376.
Pandey, V. P., Singh, S., Jaiswal, N., Awasthi, M., Pandey, B., and Dwivedi, U. N. (2013). Papaya fruit ripening: ROS metabolism, gene cloning, characterization and molecular docking of peroxidase. Journal of Molecular Catalysis B: Enzymatic, 98 (2013), 98–105.
Pandey, V. P., and Dwivedi, U. N. (2015). A ripening associated peroxidase from papaya having a role in defense and lignification: Heterologous expression and in-silico and in-vitro experimental validation. Gene, 555 (2), 438–447.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein meaasurement with the folin-phenol reagent. Analytical Biochemistry, 217 (2), 220–230.
Vetal, M. D., and Rathod, V. K. (2015). Three phase partitioning a novel technique for purification of peroxidase from orange peels (Citrus sinenses). Food and Bioproducts Processing, 94 (2014), 284–289.
Curtis, R. A., Prausnitz, J. M., and Blanch, H. W. (1998). Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes. Biotechnology and Bioengineering, 57 (1), 11–21.
Shariat, S. Z., and Aghelan, Z. (2015). Partial purification and biochemical characterization of peroxidase from rosemary (Rosmarinus officinalis L.) leaves. Advanced Biomedical Research, 4 (1), 159.
Köktepe, T., Altın, S., Tohma, H., Gülçin, İ., and Köksal, E. (2017). Purification, characterization and selected inhibition properties of peroxidase from haricot bean (Phaseolus vulgaris L.). International Journal of Food Properties, 20 (December), 1944–1953.
Hacer, Ü. E., Ramazan, K., Nalan, Ö. and Hasan, Ö. (2015). Purification and biochemical characterization of peroxidase isolated from white cabbage (Brassica oleracea var. capitata f. alba). International Journal of Food Properties, 18 (10): 2099-2109.
Balcão, V. M., and Vila, M. M. D. C. (2015). Structural and functional stabilization of protein entities: State-of-the-art. Advanced Drug Delivery Reviews, 93, 25–41.
Das, A., Shivakumar, S., Bhattacharya, S., Shakya, S., and Swathi, S. S. (2016). Purification and characterization of a surfactant-compatible lipase from Aspergillus tamarii JGIF06 exhibiting energy-efficient removal of oil stains from polycotton fabric. 3 Biotech, 6 (2), 1–8.
Pandey, V. P., Rani, J., Jaiswal, N., Singh, S., Awasthi, M., Shasany, A. K., and Dwivedi, U. N. (2017). Chitosan immobilized novel peroxidase from Azadirachta indica: Characterization and application. International Journal of Biological Macromolecules, 104, 1713–1720.
Voet, D., Voet, J., and Pratt, C. (2004). Fundamentals of Biochemistry (Third). USA: John Wiley and Sons, Inc. 1247 pages.
Nelson, D. L., and Cox, M. M. (2008). Leninger Principles of Biochemistry (5th ed.). W. H. Freeman and Company New York. 1302 pages.
Voet, D., and Voet, J. G. (2011). Biochemistry (4th ed.). John Wiley and Sons, Inc. 1772 pages.
Dahili, L. A., Kelemen-Horváth, I., and Feczkó, T. (2015). 2,4-Dichlorophenol removal by purified horseradish peroxidase enzyme and crude extract from horseradish immobilized to nano spray dried ethyl cellulose particles. Process Biochemistry, 50 (11), 1835–1842.
da Silva, B. P., Gomes Correa, R. C., Kato, C. G., de Souza, D. F., Bracht, A., and Peralta, R. M. (2017). Characterization of a Solvent-tolerant Manganese Peroxidase from Pleurotus pulmonarius and its Application in Dye Decolorization. Current Biotechnology, 6 (4), 0–1.
Elsayed, A. M., Hegazy, U. M., Hegazy, M. G. A., Abdel-Ghany, S. S., Salama, W. H., Salem, A. M. H., and Fahmy, A. S. (2018). Purification and biochemical characterization of peroxidase isoenzymes from Ficus carica latex. Biocatalysis and Agricultural Biotechnology, 16, 1–9.
Sarika, D., Kumar, P. S. S. A., Arshad, S., and Sukumaran, M. K. (2015). Original Research Article Purification and Evaluation of Horseradish Peroxidase Activity. International Journal of Current Microbiology and Applied Sciences, 4 (7), 367–375.
Gundinger, T., and Spadiut, O. (2017). A comparative approach to recombinantly produce the plant enzyme horseradish peroxidase in Escherichia coli. Journal of Biotechnology, 248 (2017), 15–24.
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