The Relationship Between Stocking Density and Sorbitol Dehydrogenase Activity in Rainbow Trout Oncorhynchus mykiss Tissues ​

Abstract

It is well known that almost all the reactions are catalyzed by enzymes in metabolism of living beings. Environmental conditions leads to very significant changes in living metabolism including fish. These changes may be genetic, hormonal, enzymatic and other physiological defects. The aim of this study was to assess the effects of increasing stock density on the activity of sorbitol dehydrogenase enzyme in liver, muscle, gill and kidney tissues of rainbow trout. Fish were reared at different stock densities 15 kg/m3, 20 kg/m3, 25 kg/m3 and 30 kg/m3 , and after adaptation period of 30 days, the experiment was carried out for two months. Stock density of the control group was 15 kg/m3. Increasing stock density caused significant inhibition of sorbitol dehydrogenase enzyme. Overall results indicate that increasing stock density significantly blocks the SDH activity in rainbow trout tissues and that this might cause undesirable results by disrupting physiological balance as inhibition of this enzyme leads to sorbitol accumulation.

Keywords

• Stock density,rainbow trout,Inhibition,sorbitol dehydrogenase

Gökkuşağı Alabalığı Oncorhynchus mykiss Dokularında Stok Yoğunluğu ve Sorbitol Dehidrogenaz Aktivitesi Arasındaki İlişki

Abstract

C anlı metabolizmasındaki hemen hemen bütün reaksiyonların enzimler tarafından katalizlendiği iyi bilinir. Çevresel şartlar, balıklarıda içine alan canlı metabolizmalarında önemli değişikliklere yol açar. Bu değişiklikler, genetic, hormonal, enzimatik, ve diğer fizyolojik eksiklikler olabilir. Bu çalışmanın amacı, artan stok yoğunluğunun gökkuşağı alabalığının karaciğer, kas, solungaç, böbrek sorbitol dehidrogenaz enzimi üzerine etkilerini belirlemektir. Balıklar farklı stok yoğunluklarında 15 kg/m3, 20 kg/m3, 25 kg/m3 ve 30 kg/m3 beslendi ve 30 günlük adaptasyon süresi sonunda deney iki ay boyunca uygulandı. Kontrol grubunun stok yoğunluğu 15 kg/m3’tür. Artan stok yoğunluğu SDH enziminin önemli oranda inhibisyonuna neden oldu. Genel sonuçlar göstermektedir ki artan stok yoğunluğu gökkuşağı alabalık dokularındaki SDH aktivitesini önemli oranda engeller ve bu da enzimin inhibisyonuna bağlı olarak artan sorbitol miktarından dolayı fizyolojik dengede istenmeyen sonuçlara neden olabilir. Böylece, enzimin inhibisyonu sorbitol birikimine öncülük eder ve fizyolojik dengenin bozulmasıyla istenmeyen sonuçlara sebep olur

Keywords

• Stok yoğunluğu,gökkuşağı alabalığı,inhibisyon,sorbitol dehidrogenaz

References

1. O. Hisar, S. Beydemir, I. Gulcin, SA. Hisar, T. Yanik, OI. Kufrevioglu, The effects of melatonin hormone on carbonic anhydrase enzyme activity in rainbow trout (Oncorhynchus mykiss) erythrocytes in vitro and in vivo, Turkish Journal of Veterinary and Animal Sciences, 29 (2005) 841.
2. H. Soyut, S. Beydemir, Purification and some kinetic properties of carbonic anhydrase from rainbow trout (Oncorhynchus mykiss) liver and metal inhibition, Protein and Peptide Letters, 15 (2005) 528.
3. I. Gulcin, S. Beydemir, O. Hisar, E. Koksal, RJ. Reiter, Melatonin administration increases antioxidant enzymes activities and reduces lipid peroxidation in the rainbow trout (Oncorhynchus mykiss, Walbaum) erythrocytes, Turkish Journal of Veterinary and Animal Sciences, 33 (2009) 241.
4. D. Ekinci, S. Beydemir, Purification of PON1 from Human Serum and Assessment of Enzyme Kinetics Against Metal Toxicity, Biological Trace Element Research, 135 (2010) 112.
5. A. Valavanidis, T. Vlahogianni, M. Dassenakis, M. Scoullos, Molecular biomarkers of oxidative stress in aquatic organisms in relation to toxic environmental pollutants, Ecotoxicology and Environmental Safety, 64 (2006) 178.
6. S. Beydemir, I. Gulcin, O. Hisar, Effect of Melatonin on glucose-6-phosphate dehydrogenase from rainbow trout (Oncorhynchus mykiss) erythrocytes in vitro and in vivo, Journal of Applied Animal Research, 28 (2005) 65. 7. I. Gulcin, A. Dastan, Synthesis of dimeric phenol derivatives and determination of in vitro antioxidant and radical scavenging activities, Journal of Enzyme Inhibition and Medicinal Chemistry, 22 (2007) 685.
7. PJ. Ashley, Fish welfare: Current issues in aquaculture, Applied Animal Behaviour Science, 104 (2007) 199.
8. T. Ellis, What is stocking density, Trout News 32 (2001) 35.

9. D. Montero, MS. Izquierdo, L. Tort, L. Robaina, JM. Vergara, High stocking density produces crowding stress altering some physiological and biochemical parameters in gilthead seabream, Sparus aurata, juveniles, Fish. Physiol. Biochem., 20 (1999) 53.
10. RW. Sodeberg, JW. Meade, Effects of rearing density on growth, survival, and fin condition af Atlantic salmon, Progr. Fish-Cult., 49 (1987) 280.
11. JC. Holm, T. Refstie, S. Bo, The effect of fish density and feeding regimes on individual growth rate and mortality in rainbow trout (Oncorhynchus mykiss), Aquaculture, 89 (1990) 225.
12. B. Björnsson, Effects of stocking density on growth rate of halibut (Hippoglossus hippoglossus L.) reared in large circular tanks for three years, Aquaculture, 123 (1994) 259.
13. MM. Vijayan, JS. Ballantyne, JF. Leatherland, High stocking density alters the energy metabolism of brook charr, Salvelinus fontinalis, Aquaculture, 88 (1990) 371.
14. A. Alanärä, E. Brännäs, Dominance-feeding behaviour in Artic charr and rainbow trout: the effect of stocking density, J. Fish Biol., 48 (1996) 242.
15. D. Ekinci, S. Beydemir, OI. Kufrevioglu, In vitro inhibitory effects of some heavy metals on human erythrocyte carbonic anhydrases, Journal of Enzyme Inhibition and Medicinal Chemistry, 22 (2007) 745.
16. H. Soyut, S. Beydemir, O. Hisar, Effects of some metals on carbonic anhydrase from brains of rainbow trout, Biological Trace Element Research, 123 (2008) 179.
17. HG. Hers, The mechanism of the transformation of glucose to fructose in seminal vesicles, Biochim. Biophys. Acta., 22 (1956) 202.
18. J. Jeffery, H. Jornvall, Sorbitol dehydrogenase, Adv. Enzymol., 61 (1988) 47.
19. RG. Tilton, K. Chang, JR. Nyengaard, Van den effects on vascular and neural dysfunction in streptozocin- induced diabetic rats, Diabetes, 44 (1995) 234.
20. K. Geisen, R. Utz, H. Grötsch, HJ. Lang, H. Nimmesgern, derivatives, Arzneimittelforschung, 44 (1994) 1032.
21. RI. Lindstad, LF. Hermansen, JS. McKinley-McKee, The kinetic mechanism of sheep liver sorbitol dehydrogenase, Eur. J. Biochem., 210 (1992) 641.
22. MM. Bradford, A rapid and sensitive method fort he quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Analitical Biochemistry, 72 (1976) 248.
23. R. Gornati, G. Terova, D. Vigetti, M. Prati, M. Saroglia, G. Bernardini, Effects of population density on seabass (Dicentrarchus labrax, L.) gene expression, Aquaculture 230 (2004) 229.
24. PD. Marco, A. Priori, MG. Finoia, A. Massari, A. Mandich, G. Marino, Physiological responses of European sea bass Dicentrarchus labrax to different stocking densities and acute stress challenge, Aquaculture, 275 (2008) 319.
25. Y. Li, J. Li, Q. Wang, The effects of dissolved oxygen concentration and stocking density on growth and non-specific immunity factors in Chinese shrimp, Fenneropenaeus chinensis, Aquaculture, 256 (2006) 608.
26. M. Funasako, K. Fujimoto, M. Taniji, T. Suruda, S. Nakai, H. Kobayashi, Y. Sakagami, M. Ohata, Effect of ageing on erythrocyte aldose reductase and sorbitol dehydrogenase activity, Mech. Ageing Dev., 73 (1994)137.
27. AP. Mizisin, L. Li, NA. Calcutt, Sorbitol accumulation and transmembrane efflux in osmotically stressed JS1 schwannoma cells, Neuroscience letters, 229 (1997) 53.