Effects of Chlorides of Lead and Some Transition Metals on the Kinetics of Crude Peroxidase from Watermelon Seeds
Journal of Advances in Biology & Biotechnology,
Aims: This study investigates the effect of chlorides of lead and some transition metals on the kinetics of crude peroxidase from watermelon seeds
Study design: In vitro enzyme assay.
Place and Duration of Study: Department of Biochemistry, Faculty of Life Sciences, Ambrose Alli University, Ekpoma, Edo State, Nigeria between April 2021 and June 2021
Methodology: The kinetics of crude peroxidase catalyzed oxidation of 3,5,3′,5′-tetramethylbenzidine (TMB) in the presence of varying concentrations of different chloride salts and hydrogen peroxidase was determined spectrophotometrically at 655nm. The assay mixture contained 2.3 mL of sodium phosphate buffer of pH 7.0, 0.1 mL of the crude enzyme from the seeds of watermelon, 0.2 mL of varying concentration of the respective chloride salts, 0.2 mL of 0.02 mM TMB, and 0.2 mL of 2 mM hydrogen peroxidase added last to start the reaction.
Results: Results showed that except for nickel chloride, chloride salts of Pb2+, Hg2+, and Fe2+ had peroxidase activating effects. Mercury chloride and lead chloride proportionately increased the enzyme activity within a salt concentration range of 1.5 and 3 mM. In comparison, ferric chloride had an optimum concentration of 2.5 mM for peroxidase activation; mercury chloride had the highest peroxidase activation effect compared with chlorides of Pb, Ni, and Fe.
Conclusion: These findings are of great importance to industries in understanding the mechanism of action of peroxidase from the seeds of watermelon, especially as the search for cheap and alternative sources of peroxidases continues.
- Transition metal
How to Cite
Godwin DC, Grover TA, Aust SD. Redox mediation in the peroxidase catalyzed oxidation of aminopyrine: Possible implications for drug-drug interactions. Chem. Res. Toxicol. 1996;9:476-483
Paradkar, V.M, Dordick; J.S. Affinity-based Reverse Micellar Extraction and Separation (ARMES): A facile technique for the purification of peroxidase from soybean hulls. Biotechnology Progress. 1993;9:199- 203.
Valderrama B, Ayala M, Vazquez – Duhalt R. Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes. Chem. Biol. 2002;9:555–565.
Hamad, I.S. Ahmed; A.A.A. Biodegradation of phenols in wastewater using crude peroxidases from five weed plants. Journal of Chemical and Pharmaceutical Research. 2013;5:60-65.
Lu, Y. Ye, W., Yang, Q., Yu, J., Wang, Q., Zhou, P., Wang, C., Xue, D., Zhao, S. Three-dimensional hierarchical porous Pt Cu dendrites: A highly efficient peroxidase nanozyme for colorimetric detection of H2O2, Sensors and Actuators B: Chemical. 2016;230:721-730.
Sonet, J. Bierla, K., Bulteau, A.L. Lobinski, R. Chavatte, L. Comparison of analytical methods using enzymatic activity, immunoaffinity and selenium-specific mass spectrometric detection for the quantitation of glutathione peroxidase 1. Analytica Chimica Acta. 2018;1011:11-19
Wang S, Wang Q, Fan X, Xu J, Zhang Y, Yuan J, Jin H, Cavaco-Paulo A. Synthesis and characterization of starch-poly(methyl acrylate) graft copolymers using horseradish peroxidase, Carbohydrate Polymers. 2016;136:1010-1016.
Xu TS. Bioconjugation of peroxidase-like nanostructures with natural enzyme for in-situ amplified conductometric immunoassay of tissue polypeptide antigen in biological fluids. Biochemical Engineering Journal. 2016;105:36-43.
Josephy PD, Eling T, Mason RP. The horseradish peroxidase-catalyzed oxidation of 3,5,3,5-tetramethylbenzidine. The Journal of Biological Chemistry. 1982;257:3669–3675.
Mahmoudi, A, Nazari, K, Mohammadian, N, Moosavi-Movahedi, A.A. Effect of Mn2+, Co2+, Ni2+, and Cu2+ on horseradish peroxidase: activation, inhibition, and denaturation studies. Appl Biochem Biotechnol. 2003;104(1):81-94.
Grafl HJ, Schwantes HO. Effect of cadmium, zinc, lead, and mercury on enzyme activity in Saccharomyces cerevisiae. Zentralbl Mikrobiol 1985; 140(1):3-11.
Bakhtawar Raza, Muhammad Javed, Faiza Ambreen, Fariha Latif. Toxic effect of lead chloride on an antioxidant enzyme in the liver and kidney of fish. J. Bioresource Manage. 2016;3(4): 1-8.
Einollahi N, Abbasi S, Dashti N, Vaezzadeh F. Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase. Iranian J Publ Health. 2006;35(2):49-56
Rimsha Nawaz, Muhammad Javed, Sidra Abbas. Safina Kousar. Effect of Iron Chloride on Peroxidase Activity in Kidney and Liver of Labeo rohita. Pakistan J. Zool. 2018;50(1): 377-380.
Atli, G., and Canli, M. Response of antioxidant system of freshwater fish Oreochromis niloticus to acute and chronic metal (Cd, Cu, Cr, Zn, Fe) exposures. Ecotoxicology and Environmental Safety. 2010;73:1884-1889.
Jacqueline Keyhani, Ezzatollah Keyhani, Sekineh Zarchipour, Hossein Tayefi-Nasrabadi, Nahid Einollahi. Stepwise binding of nickel to horseradish peroxidase and inhibition of the enzymatic activity. Biochim Biophys Acta. 2005;1722(3): 312-23.
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