Krupa S.*,
Chandan J.1, Gnanesh R.1, Lakshmikanth N.1, Rahul1 and Thejseh H.S.1
Department of Biochemistry, Jnanabharathi Campus, Bangalore University, Bangalore- 56
Jain University, J C Road, Bangalore.
Email: krupa.s@jainuniversity.ac.in
Received-03.09.2022, Revised-12.09.2022, Accepted-25.09.2022
Abstract: The enzyme carboxyl esterases was extracted from the Samanea samanseeds using different buffers at different pH. Highest activity was obtained with 33 mM phosphate buffer, pH 7.0. The enzyme assay was carried out using α-naphthyl acetate as substrate. The activity of carboxyl esterases was shown to have an optimal operating condition at pH 7.0 and a temperature of 50oC. The thermo stability of the enzyme was in the range of 7oC – 37oCwith the pH stability in the range of 4.0 – 8.0. The Km and Vmax values was determined as 0.157 mM and 1.785µM / minute. IC 50 of dicholorovas for Samanea saman esterase was found to be 2.23×10-10M. Dicholorovas was found to be an irreversible inhibitor as the time of incubation increase, the percentage of activity decreases.
Keywords: Carboxylesterases, Samanea saman, Dicholorovas, α – naphthyl acetate
REFERENCES
Abernathy, C. O. and Casida, J. E. 1973. “Pyrethroid Insecticides: Esterase Cleavage in Relation to Selective Toxicity.” Science, 179(4079):1235–36.
Aldridge, W. N. (1993). “The Esterases: Perspectives and Problems.” Chemico-Biological Interactions, 87(1–3):5–13.
Aldridge, W. N. (1953a). “Serum Esterases. I. Two Types of Esterase (A and B) Hydrolysing p-Nitrophenyl Acetate, Propionate and Butyrate, and a Method for Their Determination.” The Biochemical Journal, 53(1):110–17.
Aldridge, W. N. (1953b). “Serum Esterases. II. An Enzyme Hydrolysing Diethyl p-Nitrophenyl Phosphate (E600) and Its Identity with the A-Esterase of Mammalian Sera.” The Biochemical Journal, 53(1):117–24.
Van Asperen, K. (1962). “A Study of Housefly Esterases by Means of a Sensitive Colorimetric Method.” Journal of Insect Physiology, 8(4):401–16.
Bodor, N. and P. Buchwald (2000). “Soft Drug Design: General Principles and Recent Applications.” Medicinal Research Reviews, 20(1):58–101.
Bornscheuer, Uwe T. (2002). “Microbial Carboxyl Esterases: Classification, Properties and Application in Biocatalysis.” FEMS Microbiology Reviews, 26(1):73–81.
Casida, John E. and Gary, B. Quistad (2004). “Organophosphate Toxicology: Safety Aspects of Nonacetylcholinesterase Secondary Targets.” Chemical Research in Toxicology, 17(8):983–98.
Van Gelder, J., S. Deferme, P. Annaert, L. Naesens, E. De Clercq, G. Van den Mooter, R. Kinget and Augustijns, P. (2000). “Increased Absorption of the Antiviral Ester Prodrug Tenofovir Disoproxil in Rat Ileum by Inhibiting Its Intestinal Metabolism.” Drug Metabolism and Disposition: The Biological Fate of Chemicals, 28(12):1394–96.
Godfrey, Anthony R., Jennifer Digiacinto, and Matthew W. Davis (2011). “Single-Dose Bioequivalence of 105-Mg Fenofibric Acid Tablets versus 145-Mg Fenofibrate Tablets under Fasting and Fed Conditions: A Report of Two Phase I, Open-Label, Single-Dose, Randomized, Crossover Clinical Trials.” Clinical Therapeutics, 33(6):766–75.
Gomori, G. (1953). “Human Esterases.” The Journal of Laboratory and Clinical Medicine, 42(3):445–53.
Gupta, R. C. and Dettbarn, W. D. (1993). “Role of Carboxylesterases in the Prevention and Potentiation of N-Methylcarbamate Toxicity.” Chemico-Biological Interactions, 87(1–3):295–303.
Halpin, R. A., E. H. Ulm, A. E. Till, P. H. Kari, K. P. Vyas, D. B. Hunninghake, and D. E. Duggan. n.d. “Biotransformation of Lovastatin. V. Species Differences in in Vivo Metabolite Profiles of Mouse, Rat, Dog, and Human.” Drug Metabolism and Disposition: The Biological Fate of Chemicals, 21(6):1003–11.
Hatfield, M. Jason, Lyudmila Tsurkan, Michael Garrett, Timothy M. Shaver, Janice L. Hyatt, Carol C. Edwards, Latorya D. Hicks, and Philip M. Potter (2011. “Organ-Specific Carboxylesterase Profiling Identifies the Small Intestine and Kidney as Major Contributors of Activation of the Anticancer Prodrug CPT-11.” Biochemical Pharmacology, 81(1):24–31.
Hunter, R. L. and C. L. Markert (1957). “Histochemical Demonstration of Enzymes Separated by Zone Electrophoresis in Starch Gels.” Science (New York, N.Y.), 125(3261):1294–95.
Kao, L. R., N. Motoyama and W. C. Dauterman. (1985). “The Purification and Characterization of Esterases from Insecticide-Resistant and Susceptible House Flies.” Pesticide Biochemistry and Physiology, 23(2):228–39.
Kong, Qingkun, Yanhu Wang, Lina Zhang, Shenguang Ge, and Jinghua Yu. (2017). “A Novel Microfluidic Paper-Based Colorimetric Sensor Based on Molecularly Imprinted Polymer Membranes for Highly Selective and Sensitive Detection of Bisphenol A.” Sensors and Actuators B: Chemical, 243:130–36.
Krejci, E., N. Duval, A. Chatonnet, P. Vincens and Massoulié, J. (1991). “Cholinesterase-like Domains in Enzymes and Structural Proteins: Functional and Evolutionary Relationships and Identification of a Catalytically Essential Aspartic Acid.” Proceedings of the National Academy of Sciences of the United States of America, 88(15):6647–51.
Lowry, O. H., N. J. Rosebrough, A. L. Farr and R. J. Randall (1951). “Protein Measurement with the Folin Phenol Reagent.” The Journal of Biological Chemistry, 193(1):265–75.
MacDougall, Conan and B. Joseph Guglielmo (2004). “Pharmacokinetics of Valaciclovir.” The Journal of Antimicrobial Chemotherapy, 53(6):899–901.
Pindel, Evgenia V., Natalia Y. Kedishvili, Trent L. Abraham, Monica R. Brzezinski, Jing Zhang, Robert A. Dean and William, F. Bosron. (1997). “Purification and Cloning of a Broad Substrate Specificity Human Liver Carboxylesterase That Catalyzes the Hydrolysis of Cocaine and Heroin.” Journal of Biological Chemistry, 272(23):14769–75.
Potter, P. M., J. S. Wolverton, C. L. Morton, M. Wierdl and Danks, M. K. (1998). “Cellular Localization Domains of a Rabbit and a Human Carboxylesterase: Influence on Irinotecan (CPT-11) Metabolism by the Rabbit Enzyme.” Cancer Research, 58(16):3627–32.
Potter, Philip and Randy Wadkins (2006). “Carboxylesterases – Detoxifying Enzymes and Targets for Drug Therapy.” Current Medicinal Chemistry, 13(9):1045–54.
Putterill, Joanna J., Kim M. Plummer, Richard D. Newcomb and Sean D. G. Marshall (2003). “The Carboxylesterase Gene Family from Arabidopsis Thaliana.” Journal of Molecular Evolution, 57(5):487–500.
Quinney, S. K., S. P. Sanghani, W. I. Davis, T. D. Hurley, Z. Sun, D. J. Murry and W. F. Bosron (2005). “Hydrolysis of Capecitabine to 5’-Deoxy-5-Fluorocytidine by Human Carboxylesterases and Inhibition by Loperamide.” The Journal of Pharmacology and Experimental Therapeutics, 313(3):1011–16.
Redinbo, Matthew R. and Philip M. Potter (2005). “Mammalian Carboxylesterases: From Drug Targets to Protein Therapeutics.” Drug Discovery Today, 10(5):313–25.
Reisfeld, R. A., U. J. Lewis and Williams, D. E. (1962). “Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide Gels.” Nature, 195:281–83.
Russell, Robyn J., Colin Scott, Colin J. Jackson, Rinku Pandey, Gunjan Pandey, Matthew C. Taylor, Christopher W. Coppin, Jian-Wei Liu and John G. Oakeshott (2011). “The Evolution of New Enzyme Function: Lessons from Xenobiotic Metabolizing Bacteria versus Insecticide-Resistant Insects.” Evolutionary Applications, 4(2):225–48.
Satoh, Tetsuo and Masakiyo Hosokawa (2006). “Structure, Function and Regulation of Carboxylesterases.”Chemico-Biological Interactions, 162(3):195–211.
Satoh, Tetsuo, Palmer Taylor, William F. Bosron, Sonal P. Sanghani, Masakiyo Hosokawa and Bert N. La Du. (2002). “Current Progress on Esterases: From Molecular Structure to Function.” Drug Metabolism and Disposition: The Biological Fate of Chemicals, 30(5):488–93.
Shi, Deshi, Jian Yang, Dongfang Yang, Edward L. LeCluyse, Chris Black, Li You, Fatemeh Akhlaghi and Bingfang Yan (2006). “Anti-Influenza Prodrug Oseltamivir Is Activated by Carboxylesterase Human Carboxylesterase 1, and the Activation Is Inhibited by Antiplatelet Agent Clopidogrel.” The Journal of Pharmacology and Experimental Therapeutics, 319(3):1477–84.
Sogorb, Miguel A. and Eugenio Vilanova (2002). “Enzymes Involved in the Detoxification of Organophosphorus, Carbamate and Pyrethroid Insecticides through Hydrolysis.” Toxicology Letters, 128(1–3):215–28.
Staples, G. W. and C. R. Elevitch (2006).“Samanea Saman (Rain Tree). In: Species Profiles for Pacific Island Agroforestry.”
Stok, Jeanette E., Huazhang Huang, Paul D. Jones, Craig E. Wheelock, Christophe Morisseau and Bruce D. Hammock (2004). “Identification, Expression, and Purification of a Pyrethroid-Hydrolyzing Carboxylesterase from Mouse Liver Microsomes.” The Journal of Biological Chemistry, 279(28):29863–69.
Tang, B. K. and Kalow, W. (1995). “Variable Activation of Lovastatin by Hydrolytic Enzymes in Human Plasma and Liver. 4.” European Journal of Clinical Pharmacology, 47(5):449–51.
Testa, Bernard, and Stefanie D. Krämer (2007). “The Biochemistry of Drug Metabolism–an Introduction: Part 3. Reactions of Hydrolysis and Their Enzymes.” Chemistry & Biodiversity 4(9):2031–2122.
Tong, Leah, Truc K. Phan, Kelly L. Robinson, Darius Babusis, Robert Strab, Siddhartha Bhoopathy, Ismael J. Hidalgo, Gerald R. Rhodes and Adrian S. Ray (2007). “Effects of Human Immunodeficiency Virus Protease Inhibitors on the Intestinal Absorption of Tenofovir Disoproxil Fumarate in Vitro.” Antimicrobial Agents and Chemotherapy, 51(10):3498–3504.
Vickers, S., C. A. Duncan, I. W. Chen, A. Rosegay and Duggan, D. E. (1990). “Metabolic Disposition Studies on Simvastatin, a Cholesterol-Lowering Prodrug.” Drug Metabolism and Disposition: The Biological Fate of Chemicals, 18(2):138–45.
Williams, F. M. (1985). “Clinical Significance of Esterases in Man.” Clinical Pharmacokinetics, 10(5):392–403.
Wrigley, C. W. (1968). “Analytical Fractionation of Plant and Animal Proteins by Gel Electrofocusing.” Journal of Chromatography, 36(3):362–65.
Yang, Yue, Richard Xu, Choong-je Ma, A. Corina Vlot, Daniel F. Klessig and Eran Pichersky (2008). “Inactive Methyl Indole-3-Acetic Acid Ester Can Be Hydrolyzed and Activated by Several Esterases Belonging to the At MES Esterase Family of Arabidopsis.” Plant Physiology, 147(3):1034–45.
Yu, Quan-You, Cheng Lu, Wen-Le Li, Zhong-Huai Xiang and Ze Zhang (2009). “Annotation and Expression of Carboxylesterases in the Silkworm, Bombyx Mori.” BMC Genomics, 10(1):553.
Zhang, J., J. C. Burnell, N. Dumaual and W. F. Bosron (1999). “Binding and Hydrolysis of Meperidine by Human Liver Carboxylesterase HCE-1.” The Journal of Pharmacology and Experimental Therapeutics, 290(1):314–18.