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Tissue-Specific Esterase Isozyme Patterns in Oreochromis mossambicus (cypriniformes) and Puntius sarana (perciformes) Revealed by Zymography and Inhibitor Profiling


Authors : V. Rajaiah

Volume/Issue : Volume 11 - 2026, Issue 9 - September


Google Scholar : https://tinyurl.com/3s47hb9s

DOI : https://doi.org/10.38124/ijisrt/26sep950

Note : A published paper may take 4-5 working days from the publication date to appear in PlumX Metrics, Semantic Scholar, and ResearchGate.


Abstract : Tissue-specific esterase isozyme profiles were investigated in gill, liver, intestine, muscle, brain, and eye tissues of Oreochromis mossambicus and Puntius sarana using electrophoretic zymography and inhibitor-based classification. In O. mossambicus, three esterase zones with relative mobility (Rm) values of 0.96, 0.75, and 0.66 were detected. The Rm 0.96 zone occurred in gill, liver, and intestine and was classified as carboxylesterase (CE). The Rm 0.75 zone was present in all tissues but showed tissue-dependent classification, including CE, esterase resistant to inhibitors (ER), cholinesterase (ChE), and CHsp esterase. The Rm 0.66 zone was present in all tissues except gill and was classified mainly as ER or ChE esterase. In P. sarana, five zones with Rm values of 0.86, 0.75, 0.66, 0.50, and 0.33 were identified. Gill, liver, and intestine showed four esterase zones each, whereas muscle, brain, and eye showed three zones. The Rm 0.50 and 0.33 zones were ubiquitous in P. sarana, while the Rm 0.86 zone was restricted to intestine. ER esterases predominated in gill, liver, intestine, and brain, whereas ChE and CE esterases displayed marked tissue specificity. These findings demonstrate clear interspecific and tissue-dependent heterogeneity in esterase isozyme expression, supporting the value of zymographic inhibitor profiling for biochemical characterization and environmental biomonitoring of freshwater fishes.

Keywords : Esterase Isozymes; Zymography; Carboxylesterase; Cholinesterase; Tissue Specificity; Oreochromis mossambicus; Puntius sarana.

References :

  1. BheemRao, T., Ganesh, K., & Sanjeevaiah, A. (2024). Esterase inhibition study in different tissues (intestine, muscle and brain) of freshwater catfish Heteropneustes fossilis through polyacrylamide gel electrophoresis. Uttar Pradesh Journal of Zoology, 45(5), 120–126. https://doi.org/10.56557/upjoz/2024/v45i53937
  2. Casarett, L. J., Doull, J., & Klaassen, C. D. (Eds.). (2019). Casarett and Doull’s toxicology: The basic science of poisons (9th ed.). McGraw-Hill Education.
  3. Ellman, G. L., Courtney, K. D., Andres, V., Jr., & Featherstone, R. M. (1961). A new and rapid colorimetric determination of acetylcholinesterase activity. Biochemical Pharmacology, 7(2), 88–95. https://doi.org/10.1016/0006-2952(61)90145-9
  4. Gallego-Ríos, S. E., Peñuela, G. A., & Martínez-López, E. (2021). Updating the use of biochemical biomarkers in fish for the evaluation of alterations produced by pharmaceutical products. Environmental Toxicology and Pharmacology, 88, 103756. https://doi.org/10.1016/j.etap.2021.103756
  5. Guilhermino, L., Lopes, M. C., Carvalho, A. P., & Soares, A. M. V. M. (1996). Inhibition of acetylcholinesterase activity in juveniles of Daphnia magna exposed to the organophosphorus insecticide dimethoate. Ecotoxicology and Environmental Safety, 35(3), 279–284.
  6. Kaplan, J. G., & Nunez, J. (2019). Esterases and their relevance in aquatic toxicology. Aquatic Toxicology, 214, 105244.
  7. Lionetto, M. G., Caricato, R., & Giordano, M. E. (2013). Pollution biomarkers in environmental and human biomonitoring. The Open Environmental & Biological Monitoring Journal, 6, 1–9.
  8. Oropesa, A. L., et al. (2024). Sensitivity of cholinesterases and carboxylesterases to pharmaceutical products in Tinca tinca. Environmental Toxicology. https://doi.org/10.1002/tox.24234
  9. Peakall, D. B. (1992). Animal biomarkers as pollution indicators. Chapman & Hall.
  10. Sanchez-Hernandez, J. C., et al. (2024). B-esterase activities in several tissues of the marine fish sea bass and hake as potential biomarkers of bisphenol A derivatives. Journal of Environmental Exposure Assessment. https://doi.org/10.20517/jeea.2023.52
  11. Satoh, T., & Hosokawa, M. (2006). Toxicological implications of esterases—from molecular structures to functions. Toxicology and Applied Pharmacology, 207(2 Suppl.), 11–18. https://doi.org/10.1016/j.taap.2005.01.046
  12. Sturm, A., da Silva de Assis, H. C., & Hansen, P. D. (1999). Cholinesterases of marine teleost fish: Enzymological characterization and potential use in the monitoring of neurotoxic contamination. Marine Environmental Research, 47(4), 389–398. https://doi.org/10.1016/S0141-1136(98)00127-5
  13. van der Oost, R., Beyer, J., & Vermeulen, N. P. E. (2003). Fish bioaccumulation and biomarkers in environmental risk assessment: A review. Environmental Toxicology and Pharmacology, 13(2), 57–149. https://doi.org/10.1016/S1382-6689(02)00126-6
  14. Wheelock, C. E., Shan, G., & Ottea, J. (2005). Overview of carboxylesterases and their role in the metabolism of insecticides. Journal of Pesticide Science, 30(2), 75–83. https://doi.org/10.1584/jpestics.30.75
  15. Wheelock, C. E., Phillips, B. M., Anderson, B. S., Miller, J. L., Miller, M. J., & Hammock, B. D. (2008). Applications of carboxylesterase activity in environmental monitoring and toxicity identification evaluations. Reviews of Environmental Contamination and Toxicology, 195, 117–178. https://doi.org/10.1007/978-0-387-77030-7_5
  16. Whyte, J. J., Jung, R. E., Schmitt, C. J., & Tillitt, D. E. (2000). Ethoxyresorufin-O-deethylase (EROD) activity in fish as a biomarker of chemical exposure. Critical Reviews in Toxicology, 30(4), 347–570. https://doi.org/10.1080/10408440091159239
  17. Wang, D., Zou, L., Jin, Q., Hou, J., & Ge, G. (2018). Carboxylesterases: General detoxifying enzymes. Chemico-Biological Interactions, 289, 1–13. https://doi.org/10.1016/j.cbi.2018.04.014
  18. Ross, M. K., & Borazjani, A. (2014). Carboxylesterases: Dual roles in lipid and pesticide metabolism. Journal of Biochemical and Molecular Toxicology, 28(5), 183–197. https://doi.org/10.1002/jbt.21536
  19. Sogorb, M. A., Vilanova, E., & Carrera, V. (2004). Future applications of phosphotriesterases in the prophylaxis and treatment of organophosphorus insecticide and nerve-agent poisonings. Toxicology Letters, 151(1), 219–233. https://doi.org/10.1016/j.toxlet.2004.01.018
  20. Jovanović, B., & Guzmán, H. M. (2025). Oxidative stress and neurotoxicity biomarkers in fish toxicology. Antioxidants, 14(8), 939. https://doi.org/10.3390/antiox14080939

Tissue-specific esterase isozyme profiles were investigated in gill, liver, intestine, muscle, brain, and eye tissues of Oreochromis mossambicus and Puntius sarana using electrophoretic zymography and inhibitor-based classification. In O. mossambicus, three esterase zones with relative mobility (Rm) values of 0.96, 0.75, and 0.66 were detected. The Rm 0.96 zone occurred in gill, liver, and intestine and was classified as carboxylesterase (CE). The Rm 0.75 zone was present in all tissues but showed tissue-dependent classification, including CE, esterase resistant to inhibitors (ER), cholinesterase (ChE), and CHsp esterase. The Rm 0.66 zone was present in all tissues except gill and was classified mainly as ER or ChE esterase. In P. sarana, five zones with Rm values of 0.86, 0.75, 0.66, 0.50, and 0.33 were identified. Gill, liver, and intestine showed four esterase zones each, whereas muscle, brain, and eye showed three zones. The Rm 0.50 and 0.33 zones were ubiquitous in P. sarana, while the Rm 0.86 zone was restricted to intestine. ER esterases predominated in gill, liver, intestine, and brain, whereas ChE and CE esterases displayed marked tissue specificity. These findings demonstrate clear interspecific and tissue-dependent heterogeneity in esterase isozyme expression, supporting the value of zymographic inhibitor profiling for biochemical characterization and environmental biomonitoring of freshwater fishes.

Keywords : Esterase Isozymes; Zymography; Carboxylesterase; Cholinesterase; Tissue Specificity; Oreochromis mossambicus; Puntius sarana.

Paper Submission Last Date
31 - October - 2026

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