Authors : V. Rajaiah

Volume/Issue : Volume 11 - 2026, Issue 10 - October

Google Scholar : https://tinyurl.com/ycxss4es

DOI : https://doi.org/10.38124/ijisrt/26Oct145

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

Abstract : Estearase distribution was investigated in six tissues—gill, liver, intestine, muscle, brain, and eye—of two cypriniform fishes, Catla catla and Labeo rohita. Esterase patterns were examined by electrophoresis and the individual zones were characterized on the basis of their relative mobility (Rm) and their sensitivity to specific inhibitors. In Catla catla, esterase zones showed marked tissue-specific variation. Esterases resistant to inhibitors (ER) were widely distributed, while cholinesterase-like enzymes (CHsp), carboxylesterases (CE), cholinesterases (ChE), and arylesterases (ArE) occurred in particular tissues. In Labeo rohita, CE and ER esterases were prominent, with additional ChE, CHsp, ArE, and Esdp zones occurring in specific tissues. The results demonstrate that esterase profiles differ among tissues and between the two species, and that zones with similar electrophoretic mobility may differ in inhibitor sensitivity depending on the tissue.

Keywords : Electrophoresis; Esterases; Gill; Liver; Intestine; Muscle; Brain; Eye; Catla catla; Labeo rohita.

References :

1. Bornscheuer, U. T. (2002). Microbial carboxyl esterases: Classification, properties and applications in biocatalysis. FEMS Microbiology Reviews, 26, 73–81.
2. Cammarota, M. C., & Freire, D. M. G. (2006). A review on hydrolytic enzymes in the treatment of wastewater with high oil and grease content. Bioresource Technology, 97, 2195–2210.
3. Haritos, A. A., & Salmastrakis, S. S. (1982). A comparison of muscle esterases in the fish genus Trachurus by vertical gel electrophoresis. Comparative Biochemistry and Physiology Part B, 72, 477–480.
4. Hart, N. H., & Cook, M. (1976). Comparative analysis of tissue esterases in zebra danio (Brachydanio rerio) and the pearl danio (B. albolineatus) by disc gel electrophoresis. Comparative Biochemistry and Physiology Part B, 54, 357–364.
5. Hasan, F., Shah, A. A., & Hameed, A. (2006). Industrial applications of microbial lipases. Enzyme and Microbial Technology, 39, 235–251.
6. Holmes, R. S., & Masters, C. J. (1967). The developmental multiplicity and isoenzyme status of cavian esterases. Biochimica et Biophysica Acta, 132, 379–399.
7. Jaeger, K. E., & Eggert, T. (2002). Lipases for biotechnology. Current Opinion in Biotechnology, 13(4), 390–397.
8. Lakshmipathi, V., & Reddy, T. M. (1989). Esterase polymorphisms in muscle and brain of four freshwater fishes belonging to the family Cyprinidae. Journal of Applied Ichthyology, 5(2), 88–95.
9. Loevenhart, A. S. (1906). Journal of Biological Chemistry, 2, 427. (Quoted by Pearse, 1972).
10. Maurer, K. (2004). Detergent proteases. Current Opinion in Biotechnology, 15, 330–334.
11. Yu, Q. Y., Lu, C., Li, W. L., Xiang, Z. H., & Zhang, Z. (2009). Annotation and expression of carboxylesterases in the silkworm, Bombyx mori. BMC Genomics, 10, 553.
12. Rao, M. B., Tanksale, A. M., Ghatge, M. S., & Deshpande, V. V. (1998). Molecular and biotechnological aspects of microbial proteases. Microbiology and Molecular Biology Reviews, 62, 597–635.
13. Reetz, M. T. (2002). Lipases as practical biocatalysts. Current Opinion in Chemical Biology, 6, 145–150.
14. Seligman, A. M., & Nachlas, M. M. (1950). Journal of Clinical Investigation, 29, 31. (Quoted by Pearse, 1972).
15. Sharma, R., Chisti, Y., & Banerjee, U. C. (2001). Production, purification, characterization and applications of lipases. Biotechnology Advances, 19, 627–662.
16. Pereira, B. V. R., Silva-Zacarin, E. C. M., Costa, M. J., dos Santos, A. C. A., do Carmo, J. B., & Nunes, B. (2019). Cholinesterases characterization of three tropical fish species, and their sensitivity towards specific contaminants. Ecotoxicology and Environmental Safety, 173, 482–493. https://doi.org/10.1016/j.ecoenv.2019.01.105
17. Martínez-Morcillo, S., Pérez-López, M., Míguez, M. P., Valcárcel, Y., & Soler, F. (2019). Comparative study of esterase activities in different tissues of marine fish species Trachurus trachurus, Merluccius merluccius and Trisopterus luscus. Science of the Total Environment, 679, 12–22. https://doi.org/10.1016/j.scitotenv.2019.05.047
18. Lan, L., Ren, X., Yang, J., Liu, D., & Zhang, C. (2020). Detection techniques of carboxylesterase activity: An update review. Bioorganic Chemistry, 94, 103388. https://doi.org/10.1016/j.bioorg.2019.103388
19. Park, J. M., Won, S. M., Kang, C. H., Park, S., & Yoon, J. H. (2020). Characterization of a novel carboxylesterase belonging to family VIII hydrolyzing β-lactam antibiotics from a compost metagenomic library. International Journal of Biological Macromolecules, 164, 4650–4661. https://doi.org/10.1016/j.ijbiomac.2020.09.070
20. Santana, M. S., Sandrini-Neto, L., Di Domenico, M., & Prodocimo, M. M. (2021). Pesticide effects on fish cholinesterase variability and mean activity: A meta-analytic review. Science of the Total Environment, 757, 143829. https://doi.org/10.1016/j.scitotenv.2020.143829
21. Johan, U. U. M., Raja Abd Rahman, R. N. Z., Kamarudin, N. H. A., & Ali, M. S. M. (2021). An integrated overview of bacterial carboxylesterase: Structure, function and biocatalytic applications. Colloids and Surfaces B: Biointerfaces, 205, 111882. https://doi.org/10.1016/j.colsurfb.2021.111882
22. Olivares-Rubio, H. F., & Espinosa-Aguirre, J. J. (2021). Acetylcholinesterase activity in fish species exposed to crude oil hydrocarbons: A review and new perspectives. Chemosphere, 264, 128401. https://doi.org/10.1016/j.chemosphere.2020.128401
23. Santana, M. S., Domingues de Melo, G., Sandrini-Neto, L., Di Domenico, M., & Prodocimo, M. M. (2022). A meta-analytic review of fish antioxidant defense and biotransformation systems following pesticide exposure. Chemosphere, 291, 132730. https://doi.org/10.1016/j.chemosphere.2021.132730
24. Nanthanawat, P., Kiatprasert, P., Wattanakornsiri, A., Nanuam, J., Prasatkaew, W., Ruttanakorn, S., & Thanomsit, C. (2022). Development of an antibody technique for acetylcholinesterase expression detection in the gill of Nile tilapia (Oreochromis niloticus) as a glyphosate-based herbicide biomarker. Toxicology Reports, 9, 1548–1556. https://doi.org/10.1016/j.toxrep.2022.07.009
25. Solé, M., Rivera-Ingraham, G., & Freitas, R. (2018). The use of carboxylesterases as biomarkers of pesticide exposure in bivalves: A methodological approach. Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology, 212, 18–24. https://doi.org/10.1016/j.cbpc.2018.06.002
26. Solé, M., & Sanchez-Hernandez, J. C. (2018). Elucidating the importance of mussel carboxylesterase activity as exposure biomarker of environmental contaminants of current concern: An in vitro study. Ecological Indicators, 85, 432–439. https://doi.org/10.1016/j.ecolind.2017.10.046
27. Ghodke, P., et al. (2022). Environmental role of aromatic carboxylesterases. Environmental Microbiology. https://doi.org/10.1111/1462-2920.15774
28. Ekeoma, B. C., Ekeoma, L. N., Yusuf, M., Haruna, A., Ikeogu, C. K., Merican, Z. M. A., Kamyab, H., Pham, C. Q., Vo, D.-V. N., & Chelliapan, S. (2023). Recent advances in the biocatalytic mitigation of emerging pollutants: A comprehensive review. Journal of Biotechnology, 369, 14–34. https://doi.org/10.1016/j.jbiotec.2023.05.003
29. Gajula, S. K., Kanthala, S. K., Narra, M. R., & Vanamala, V. D. (2023). Individual and interactive biochemical profile damages in Labeo rohita (Cyprinidae) by imidacloprid and clothianidin. Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology, 271, 109689. https://doi.org/10.1016/j.cbpc.2023.109689
30. Sürmeli, Y., Vardar-Yel, N., & Tütüncü, H. E. (2025). Recent advances of structure, function, and engineering of carboxylesterases for the pharmaceutical industry: A minireview. International Journal of Biological Macromolecules, 307(Pt 3), 142206. https://doi.org/10.1016/j.ijbiomac.2025.142206.