Identification of some biochemical indicators to indicate the contamination of some fish farms in Hilla city/ Iraq

Authors

  • Layla Mustafa A.A. Alkatrani Environmental Research & Study Center, University of Babylon, Babylon, Iraq. https://orcid.org/0000-0002-1275-100X
  • Zahraa Hussein Obaid Environmental Research & Study Center, University of Babylon, Babylon, Iraq. https://orcid.org/0000-0003-1558-1680
  • Jasim Mohammed Salman Department of Biology, College of Science, University of Babylon, Babylon, Iraq.

DOI:

https://doi.org/10.21123/bsj.2024.9312

Keywords:

antioxidants, biochemical indicator, common carp, contamination, Oxidative stress.

Abstract

In order to establish the possibility of determined biochemical indicators of possible pollution in Al-Forat fish farm (A) and Hussein Ajimi fish farm (B) as well as wild fish samples as a control from Shatt Al-Hilla River (C). Oxidative stress factors and antioxidant enzyme activity were determined in common carp Cyprinus carpio blood serum from two fish farms. Reactive Oxygen Species (ROS), Superoxide Dismutase (SOD), Catalase (CAT), Glutathione peroxidase (GPx) and Hydrogen peroxide (H2O2) performance were chosen as pollution bioindicators, as well as Total Protein (TP) as a general bio indicator for fish health. Results showed an increase in all antioxidant enzymes activities and oxidative stress factors in fishes from station B which recorded 34.52 μg/ml, 81.46 U/ml, 75.55 KU/L, 4.36 ± 0.4 U/l, 11.82 nmol and 41.13 mg/l for ROS, SOD, CAT, GPx, H2O2 and TP respectively in a significant difference (P < 0.05) from stations A and C, which indicate the heighten of pollution in the Hussein Ajimi fish farm B than from Al-Forat fish farm A and the control fish from Shatt Al-Hilla River C. The study confirms the possibility of using oxidative stress factors and antioxidant enzymes as biochemical indicators of fish farms pollution.

References

Abhijith BD, Ramesh M, Poopal RK. Responses of metabolic and antioxidant enzymatic activities in gill, liver and plasma of Catla catla during methyl parathion exposure. J. basic appl zool. 2016; 77: 31-40. http://dx.doi.org/10.1016/j.jobaz.2015.11.002

Correia AD, goncalves R, Scholze M, Ferreira M, Henrigues MA. Biochemical and behavioral responses in gill head seabream (Sperus auratus) to phenanthrene. J Exper Marine Boil Ecology. 2007; 347: 109-22. http://doi.org/10.1016/j.jembe.2007.03.015

Sun YY, Yu HX, Zhang JF, Yin Y, Shi HH, Wang XR. Bioaccumulation, depuration and oxidative stress in fish Carassius auratus under phenanthrene exposure. Chemosphere. 2006; 63: 1319-27. http://doi.org/10.1016/j.chemosphere.2005.09.032

Gad NS. Oxidative stress and antioxidant enzymes in Oreochromis niloticus as biomarkers of exposure to crude oil pollution. International Journal of Environmental Science and Engineering (IJESE). 2011; 1: 49-58.

Velkova-Jordanoska L, Kostoski G, Jordanoska B. Antioxidative enzymes in fish as biochemical indicators of aquatic pollution. Bulg J Agric Sci. 2008; 14 (2): 235-37.

Lokken VK. Antioxidant Enzyme System in Fish from Contaminated Lakes in Chernobyl Exclusion Zone. MSc. Thesis, Faculty of Environmental Sciences and Natural Resource Management, Norwegian University of life science, Norway; 2020: 64 p.

Shaliutina-Kolesova A, Gazo I, Cosson J, Linhart O. Comparison of oxidant and antioxidant status of seminal plasma and spermatozoa of several fish species. Czech J Anim Sci. 2013; 58: 313–20. https://doi.org/10.17221/6861-CJAS

Shaliutina-Kolesova A, Xian M, Nian R. Antioxidant defence system in protein fractions of common carp (Cyprinus carpio) seminal plasma. Czech J Anim Sci. 2019; 64(6): 265-71. https://doi.org/10.17221/187/2018-CJAS

Finosh GT, Jayabalan M. Reactive oxygen species control and management using amphiphilic biosynthetic hydrogels for cardiac applications. Adv biosci biotechnol. 2013; 4: 1134-46. http://dx.doi.org/10.4236/abb.2013.412150

Aitken RJ. The Amoroso Lecture. The human spermatozoon – a cell in crisis? J Reprod Fertil.. 1999; 115: 1–7. https://doi.org/10.1530/jrf.0.1150001

Shi Q, Xiong X, Wen Z, Qin C, Li R, Zhang Z, et al. Cu/Zn Superoxide dismutase and catalase of yangtze sturgeon, Acipenser dabryanus: molecular cloning, tissue distribution and response to fasting and refeeding. Fishes. 2022. 7(1): 35. https://doi.org/10.3390/fishes7010035

Tiwari MK, Hägglund PM, Moller IM, Davies MJ, Bjerrum MJ. Copper ion /H2O2 oxidation of Cu/Zn-Superoxide dismutase: Implications for enzymatic activity and antioxidant action. Redox Biol. 2019; 26: 101262. https://doi.org/10.1016/j.redox.2019.101262

Gomez-Anduro GA, Barillas-Mury CV, Peregrino-Uriarte AB, Gupta L, Gollas-Galvan T, Hernandez-Lopez J, et al. The cytosolic manganese superoxide dismutase from the shrimp Litopenaeus vannamei: Molecular cloning and expression. Dev Comp Immunol. 2006; 30: 893–900. https://doi.org/10.1016/j.dci.2006.01.002

Martins D, English AM. SOD1 oxidation and formation of soluble aggregates in yeast: Relevance to sporadic ALS development. Redox Biol. 2014; 2: 632–9. https://doi.org/10.1016/j.redox.2014.03.005

Ighodaro OM, Akinloye OA. First line defence antioxidants superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx): Their fundamental role in the entire antioxidant defense grid. Alexandria J Med. 2018; 54 (4): 287-93. https://doi.org/10.1016/j.ajme.2017.09.001

Nandi A, Yan LJ, Jana CK, Das N. Role of Catalase in Oxidative Stress and Age-Associated Degenerative Diseases. Oxid Med Cell. Longev.. 2019; 2019, Article ID 9613090: 19 p. https://doi.org/10.1155/2019/9613090

Olson KR, Gao Y, DeLeon ER, Arif M, Arif F, Arora N, et al. Catalase as a sulfide-sulfur oxido-reductase: An ancient (and modern?) regulator of reactive sulfur species (RSS). Redox Biol. 2017; 12: 325–39. https://doi.org/10.1016/j.redox.2017.02.021

Ismail NA, Okasha SH, Dhawan A, Abdel-Rahman AO, Shaker OG, Sadik NA. Antioxidant enzyme activities in hepatic tissue from children with chronic cholestatic liver disease. Saudi J Gastroenterol . 2010; 16(2): 90-4. https://doi.org/10.4103/1319-3767.61234

Mulgund A, Doshi S, Agarwal A. Chapter 25 - The Role of Oxidative Stress in Endometriosis. In Watson, R. R. (ed.) Handbook of Fertility, San Diego: Academic Press. 2015; pp. 273-81. https://doi.org/10.1016/B978-0-12-800872-0.00025-1

Mhaisen FT, Al-Niaeem KS, Al-Zubaidy AB. Literature review on fish parasites of Al-Furat fish farm, Babylon province, Iraq. Iraqi J Aquacult. 2012; 9(1): 95-122. https://doi.org/10.21276/ijaq.2012.9.1.7

Mhaisen FT, Al-Rubaie AL. Checklists of Parasites of Farm Fishes of Babylon Province, Iraq. J Parasitol Res. 2016; 2016: 1-15. https://doi.org/10.1155/2016/7170534

Durville P, Collet A. Clove oil used as an anesthetic with juvenile tropical marine fish. SPC Live Reef Fish Information Bulletin 9. 2001; pp. 17–9.

Erel O. A new automated colorimetric method for measuring total oxidant status. Clin. Biochem. 2005; 38: 1103–11. https://doi.org/10.1016/j.clinbiochem.2005.08.008

Velikova V, Yordanov I, Edreva A. Oxidative stress and some antioxidant systems in acid rain-treated bean plants, protective role of exogenous polyamines. Plant Sci. 2000; 151: 59–66. https://doi.org/10.1016/S0168-9452(99)00197-1

Marklund S, Marklund G. Involvement of the superoxide anion radical in the autooxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem. 1974; 47: 469-74. https://doi.org/10.1111/j.1432-1033.1974.tb03714.x

Goth L. A simple method for determination of serum catalase activity and revision of reference range. Clin Chim Acta. 1991; 196: 143-52. https://doi.org/10.1016/0009-8981(91)90067-m

Hafeman DG, Sunde RA, Hoekstra WG. Effect of dietary selenium on erythrocyte and liver glutathione peroxidase in the rat. J Nutr. 1974; 104: 580-7. https://doi.org/10.1093/jn/104.5.580

Lowry OH, Rose Brough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193: 265-75. https://doi.org/10.1016/S0021-9258(19)52451-6

Batt J, Bennett-Steward K, Couturier C, Hammell L, Harvey-Clark C, Kreiberg H, et al. CCAC guidelines on: the care and use of fish in research, teaching and testing. Ottawa, ON, Canadian Council on Animal Care CCAC, Canada. 2005: 87 .

Stell RGD, Torrie JH, Dikey DA. Principles and procedures of statistics. A biometrical approach, 3rd ed., pp. 352–58. New York: McGraw Hill, Inc. Book Co. 1997.

Karadag H, Firat O, Firat O. Use of Oxidative Stress Biomarkers in Cyprinus carpio L. for the Evaluation of Water Pollution in Ataturk Dam Lake (Adiyaman, Turkey). Bull Environ Contam Toxicol. 2014; 92: 289–93. https://doi.org/10.1007/s00128-013-1187-0

Kitto MR, Tabish M. Aquaculture and Food Security in Iraq. Aquac Asia. 2004; IX (1): 31-3.

Borkovic SS, Pavlovic SZ, Kovacevic TB, Stajn AS, Petrovic VM, Saicic ZS. Antioxidant defence enzyme activities in hepatopancreas, gills and muscle of Spiny cheek crayfish (Orconectes limosus) from the River Danube. Comp Biochem Physiol. 2008; 147 Part C: 122–28. https://doi.org/10.1016/j.cbpc.2007.08.006

Kolesova ASh, Rui N, Ashtiani S, Rodina M, Cosson J, Linhart O. Oxidative Stress and Antioxidant Enzyme Defence System in Seminal Plasma of Common Carp (Cyprinus carpio) and Rainbow Trout (Oncorhynchus mykiss) during Spawning Season. Czech J Anim Sci. 2018; 63(2): 78–84. https://doi.org/10.17221/89/2017-CJAS

Valon M, Valbona A, Fahri G, Qenan M, Dhurat K, Fatmir C. Evaluating Environmental Pollution by Applying Oxidative Stress Biomarkers as Bioindicators of Water Pollution in Fish. Pol J Environ Stud. 2013; 22 (5): 1519-23.

Alkatrani LM, Yesser AKT, Al-Adub AHY (2014). Estimating some physiological parameters in the blood of Tilapia zillii fingerlings during adaptation to different salinities. Mesopot. J Mar Sci. 2014; 29(2): 115-36. https://doi.org/10.58629/mjms.v29i2.130

Akram R, Iqbal R, Hussain R, Jabeen F, Ali M. Evaluation of Oxidative stress, antioxidant enzymes and genotoxic potential of bisphenol A in fresh water bighead carp (Aristichthys nobils) fish at low concentrations. Environ Pollut. 2021; 268 (A): 115896. https://doi.org/10.1016/j.envpol.2020.115896

Fernandes C, Fontainhas-Fernandes A, Ferreira M, Salgado MA. Oxidative Stress Response in Gill and Liver of Liza saliens, from the Esmoriz-Paramos Coastal Lagoon, Portugal. Arch. Environ. Contam Toxicol. 2008; 55: 262–9. https://doi.org/10.1007/s00244-007-9108-z

Radovanovic TB, Mitic SB, Perendija BR, Despotovic SG, Pavlovic SZ, Cakic PD, et al. Superoxide dismutase and catalase activities in the liver and muscle of barbel (Barbus barbus) and its intestinal parasite (Pomphoryinchus laevis) from the Danube river, Serbia Arch Biol Sci. Belgrade. 2010; 62(1): 97-105. https://doi.org/10.2298/ABS1001097R

Sun YY, Yu H X, Zhang JF, Yin Y, Shi HH, Wang XR. Bioaccumulation, depuration and oxidative stress in fish Carassius auratus under phenanthrene exposure. Chemosphere. 2006; 63: 1319-1327. https://doi.org/10.1016/j.chemosphere.2005.09.032

Downloads

Issue

Section

article

How to Cite

1.
Identification of some biochemical indicators to indicate the contamination of some fish farms in Hilla city/ Iraq. Baghdad Sci.J [Internet]. [cited 2024 Jun. 14];21(12). Available from: https://bsj.uobaghdad.edu.iq/index.php/BSJ/article/view/9312