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Published: 2021-12-27

Page: 936-946


Department of Zoology, Khalsa College Amritsar, Amritsar, Punjab-143005, India.


Department of Zoology, Guru Nanak Dev University, Amritsar, Punjab-143005, India.

*Author to whom correspondence should be addressed.


Labeo rohita fingerlings (7.6 – 11.3 cm length and 16.1 – 26.7 g weight) were exposed for 96h to 0, 0.2 (LC10), 0.4 (LC30), 0.6 (LC55), 0.8 and 1 mg/l of Basic violet-1 (BV-1, CI No. 42535), a widely used azo dye in dyeing and textile industries. Antioxidant/detoxification enzymes such as glutathione-s-transferase (GST), glutathione reductase (GR), glutathione peroxidase (GPx), catalase (CAT) and superoxide dismutase (SOD) were estimated in liver, kidney, gill, muscle and brain of the fish as markers for the stress of BV-1. After 96h, the fish were kept for a recovery period of 30 days and activity of enzymes was determined at 15 day intervals. Significant dose dependent increase over control in the activity of GR was observed in all the tissues while a significant decrease over control was observed in SOD activity in all the tissues. The results indicate that the dye is very toxic to L. rohita as there was a marked change in the activity of selected enzymes in the exposed fish. Gill was maximally affected tissue whereas GR was maximally affected enzyme and the effect prolonged till the end of recovery period. So this enzyme in gill can be considered as best biomarker to determine toxicity of even very low doses of the azo dye BV-1 in fish.

Keywords: L. rohita, basic violet-1, azo dye, brain, antioxidant enzymes, detoxification

How to Cite

KAUR, S., & KAUR, A. (2021). EFFECT OF ACUTE DOSES OF BASIC VIOLET-1 (BV-1) ON ANTIOXIDANT/DETOXIFICATION ENZYMES OF Labeo rohita. UTTAR PRADESH JOURNAL OF ZOOLOGY, 42(24), 936–946. Retrieved from https://mbimph.com/index.php/UPJOZ/article/view/2807


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Puvaneswari N, Muthukrishnan J, Gunasekaran P. Toxicity assessment microbial degradation of azo dyes. Indian J. Exp. Biol., 2006;44(8):618-626.

Banat IM, Nigam P, Singh D, Marchant R. Microbial decolorization of textile-dye containing effluents – a review. Bioresour. Technol. 1996;58:217–227.

Zollinger H. Colour chemistry- synthesis, properties and applications of organic dyes and pigments. VCH, New York. 1987;92.

Halliwell B, Gutteridge JMC. Free Radicals in Biology and Medicine. Clarendon Press, Oxford, 1989;543.

Wilhelm Filho D. Fish antioxidant defenses: A comparative approach. Braz. J. Med. Biol. Res., 1996;29:1735-1742.

Doyotte A, Cossu C, Jacquin M, Babut M, Vasseur P. Antioxidant enzymes, glutathione and lipid peroxidation as relevant biomarkers of experimental or field exposure in the gills and the digestive gland of the freshwater bivalve Unio tumidus. Aquat. Toxicol. 1997;39:93–110.

Gamble SC, Goldfarb PS, Porte C, Livingstone DR. Glutathione Peroxidase and other antioxidant enzyme function in marine invertebrates (Mytilus edulis, Pecten maximus, Carcinus maenas and Asterias rubens). Mar. Environ. Res. 1995;39:191–195.

Stegeman JJ, Brouwer M, Di Giulio RT, Fo¨ rlin L, Fowler BA, Sanders BM, Van Veld PA. Molecular responses to environmental contamination: enzyme and protein systems as indicators of chemical exposure and effect. In: Huggett RJ, Kimerle R, Mehrle PM, Bergman H.L. (Eds.), Biomarkers, Biochemical, Physiological, and Histological Markers of Anthropogenic Stress. Lewis, USA. 1992;235–335.

Xu L, Zheng GJ, Lam PKS, Richardson BJ. Relationship between tissue concentrations of polycyclic aromatic hydrocarbons and DNA adducts in green-lipped mussels (Perna viridis). Ecotoxicology. 1999;8:73–82.

Chien C, Dauterman WC. Studies on glutathione-S-transferase in Helicoverpa (Heliothis) zea. Insect Biochem. 1991;21(8):857-864.

Carlberg I, Mannervik B. Purification and characterization of flavoenzyme glutathione reductase from rat liver. J. Biol. Chem. 1975;250:5475-5480.

Flohe L, Gunzler WA. Glutathione Peroxidase. In: Packer, L. (Ed.), Methods in Enzymology. Academic press, New York. 1984; 105:115-121.

Bergmeyer HU. Methods of enzyme analysis. Vol I. Academic press. Inc. New York. 1974;1:438.

Kono Y. Generation of superoxide radical during autooxidation of hydroxylamine and an assay for superoxide dismutase. Arch. Biochem. Biophys. 1978;186:189-195.

Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with folin phenol reagent. J. Biochem. 1951;193:265–275.

Zhu LS, Shao B, Song Y, Xie H, Wang J, Wang JH, Liu W, Hou XX. DNA damage and effects on antioxidative enzymes in zebra fish (Danio rerio) induced by atrazine. Toxicol Mech. Methods. 2011;21(1):31–36.

Fournier D, Bride JM, Poirie M, Berge JB, Plapp FW. Insect glutathione-s-transferases: biochemical characteristics of the major forms of houseflies susceptible and resistant to insecticides. J. Biol. Chem. 1992;267:1840-1845.

Oh SH, Lee MH. Effect of p-Dimethylaminoazobenzene and 2(3)-tert-Butyl-4-hydroxyanisole on lipid peroxidation, Glutathione-S-transferase, peroxidase and reductase in rat liver. Yonsei Med. J. 1981; 22(2):95-100.

Sun Y, Yu H, Zhang J, Yin Y, Shen H, Liu H, Wang X. Bioaccumulation and antioxidant responses in goldfish Carassius auratus under HC Orange No. 1 exposure. Ecotoxicol. Environ. Saf. 2006;63:430-437.

Peng S, Xing Y, Rui L, Jian-ping C. Effects of Nitrobenzene on Liver Antioxidant Defense System of Carassius auratus. Chem. Res. Chin. Uni. 2010;26(2):204—209.

Vander oost R, Beyer J, Vermeulen PE. Fish bioaccumulation and biomarkers in enviormental risk assessment: a review. Environ. Toxicol. Pharmacol. 2003;13:57-149.

Beyer J, Sandvik M, Hylland K, Fjeld E, Egaas E, Aas E, Skare JU, Goksoyr A. Contaminant accumulation and biomarker responses in flounder (Platichthys flesus L.) and Atlantic cod (Gadus morhua L.) exposed by caging to polluted sediments in Sorfjorden, Norway. Aquat. Toxicol. 1996;36:75-98.

Grinwis GCM, Besselink HT, Van der Brandof EJ, Bulder AS, Engelsma MY, Kuiper RV, Wester PW, Vaal MA, Vethaal AD, Vos JC. Toxicity of TCDD in European flounder (Platichthys flesus) with emphasis on histopathology and cytochrome P450 1A induction in several organ systems. Aquat. Toxicol. 2000;50:387-401.

Stephensen E, Svavarsson J, Sturve J, Ericson G, Adolfsson-Erici M, Forlin L. Biochemical indicators of pollution exposure in Shorthorn sculpin (Myoxocephalus scorpius) caught in four harbours on the Southwest coast of Iceland. Aquat. Toxicol. 2000;48:431-442.

Monteiro M, Quintaneiro C, Pastorinho M, Pereira ML, Morgado F, Guilhermino L, Soares AMVM. Acute effects of 3,4-dichloroaniline on biomarkers and spleen histology of the common goby Pomatoschistus microps. Chemosphere. 2006;62:1333–1339.

Wenjuan, Z., Wei, L., Jing, Z., Huimin, Z., Yaobin, Z., Xie, Q. and Yihe, J. (2012), Characterisation of acute toxicity, genotoxicity and oxidative stress posed by textile effluent on zebrafish. J. Environ. Sci., 11, 1963-1971.

Lushchak OV, Kubrak OI, Storey JM, Storey KB, Lushchak VI. Low toxic herbicide Roundup induces mild oxidative stress in goldfish tissues. Chemosphere. 2009;76:932–937.

Modesto KA, Martinez BBR. Effects of Roundup Transorb on fish: Hematology, antioxidant defenses and Acetylcholinesterase activity. Chemosphere. 2010;81:781-787.

Li ZH, Zlabek V, Velisek J, Grabic R, Machova J, Randak T. Modulation of antioxidant defense system in brain of rainbow trout (Oncorhynchus mykiss) after chronic carbamazepine treatment. Comp. Biochem. Physiol. C. 2010;151:137–141.

Visweswaran B, Krishnamoorthy G. Oxidative Stress by Tartrazine in the Testis of Wistar Rats. J. Pharm. Biol. Sci., 2012;2(3):44-49.

Petrivalsky M, Machala M, Nezveda K, Piacka V, Svobodova Z, Drabek P. Glutathione-dependent detoxifying enzymes in rainbow trout liver: search for specific biochemical markers of chemical stress. Environ. Toxicol. Chem.1997;16(7):1417-1421.

Winston GW, Di Giulio RT. Prooxidant and antioxidant mechanisms in aquatic organisms. Aquat. Toxicol. 1991;19:137-161.

Lenartova V, Holovska K, Pedrajas JR, Martinez-Lara E, Peinado J, Lopez-Barea J, Rosival I, Kosuth P. Antioxidant and detoxifying fish enzymes as biomarkers of river pollution. Biomarkers, 1997;2:247-252.

Vijayavel K, Gomathi RD, Durgabhavani K, Balasubramanian MP. Sublethal effect of naphthalene on lipid peroxidation and antioxidant status in the edible marine crab Scylla serrate. Mar. Pollut. Bull. 2004; 48:429–433.

Santos MA, Pacheco M, Ahmad I. Anguilla Anguilla L. antioxidants responses to in situ bleached kraft pulp mill effluent outlet exposure. Environ. Int. 2004;30:301.

Shi H, Sui Y, Wang X, Luo Y, Ji L. Hydroxyl radical production and oxidative damage induced by cadmium and naphthalene in liver of Carassius auratus. Comp. Biochem. Physiol. C. 2005;140:115–121.

Yin Y, Jia H, Sun Y, Yu H, Wang X, Wu J, Xue Y. Bioaccumulation and ROS generation in liver of Carassius auratus, exposed to phenanthrene. Comp. Biochem. Physiol. C. 2007;145:288–293.

Liu H, Yu H, Giesy JP, Xu T, Zhou Y. Response of antioxidant parameters to 3,3’-dimethyl-benzidinein goldfish (carassius auratus) liver. Fresen. Environ. Bull. 2009; 18:737-743.

Zagal A, Mazmanci B. Oxidative stress response in Nile tilapia (Oreochromis niloticus) exposed to textile mill effluent. Toxicol. Ind. Health. 2011;27(1):81-85.

Vega-Lopez A, Jimenez-Orozco FA, Jimenez-Zamudio LA, Garcia-Latorre EA, Dominguez-Lopez ML. Prooxidant and antioxidant sex-linked response and its relationship to mixed oxidase function enzymes in liver of Ameca splendens, an endangered goodied fish exposed to PCBs. Toxicol. Environ. Chem., 2009;91(2):315-330.

Yonar ME, Yonar SM. Changes in selected immunological parameters and antioxidant status of rainbow trout exposed to malachite green (Oncorhynchus mykiss, Walbaum, 1792). Pestic. Biochem. Physiol. 2010;97:19-23.

Vasanth S, Ganesh A, Vijayakumar TS, Karthikeyeni S, Manimegalai M, Subramanian P. Assessment of anthracene on hepatic and antioxidant enzyme activities in Labeo rohita (Hamilton, 1822). Int. J. Pharm. Life Sci. 2012;3(5):1696-1704.

Kono Y, Fridovich I. Superoxide radical inhibits Catalase. J. Biol. Chem. 1982;257 :5751-5754.

Bainy ACD, Saito E, Carvalho PSM, Junqueira VBC. Oxidative stress in gill, erythrocytes, liver and kidney of Nile tilapia (Oreochromis niloticus) from a polluted site. Aquat. Toxicol. 1996;34:151-162.

Ayoola SO, Bassey BO, Alimba CG, Ajani EK. Textile effluent induced genotoxic effects and oxidative stress in Clarias gariepinus. Pak. J. Biol. Sci. 2012;15(17):804-812.

Hodgson EK, Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme. Biochemistry. 1975;14:5294-5299.