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1703484 Vol 5 · Issue 12 Download Paper

Temperature and pH Stability of Crude Rhodanese Enzyme Extracted from Synodontis schall

Ebizimor Wodu Ayibaene Frank-Oputu

Subject area: Science,Engineering and Technology  ·  Area of research: Enzyme Biochemistry

Abstract

This research investigates the effect of temperature and pH on the stability of the enzyme extracted from the gills and liver of Synodontis schall. Rhodanese activity was assayed by measuring the amount of product formed in ?moles at 37?C and pH 8.2 per minute. The pH stability was done with pH 5.5 ? 10.0, while 20 - 60?Cwas used to determine temperature stability. The results showed that gills rhodanese was stable within the range of pH 7.5 to 9.0, while the liver enzyme was stable within the pH range of 7.5 to 9.5. Both enzymes were stable at 30 and 400C. At 500C also the liver rhodanses was stable after incubating for 40mins, but lose 60% of its activity as the time of incubation increased. Rhodanese from the gills was not stable at higher temperatures as it loses more than 60% of its initial activity upon incubation for 10mins.

References

[1] Bonner, P.L.R. (2018) Protein Purification. 2nd ed. Taylor & Francis.

[2] Ehigie, A. F., Abdulrasak, M. A., Adeleke, G. E., & Ehigie, O. L. (2019) Comparison of Rhodanese Activity and Distribution in Tomato (Solanum lycopersicum Mill.) Plant Parts and its Physicochemical Characterization. J Plant Biochem Physiol, 7, 240. doi: 10.35248/2329 9029.19.7.240.

[3] Eskandarzade, N., Aminlari, M., Golami, S., & Tavana, M. (2012). Rhodanese activity in different tissues of the ostrich. British Poultry Science, 53(2), 270-273.

[4] Ezzi, M.I., Pascual, J.A., Gould, B.J. and Lynch, J.M. (2003). Characterisation of the rhodanese enzyme in Trichoderma

[5] Gafar, A. T., Nelson, A.A. and Kayode, A.F. (2014) Properties of rhodanese from the liver of tilapia, Oreochromis niloticus, in Asejire Lake, Nigeria. African Journal of Biochemistry Research. 8(3) 74-83. DOI: 10.5897/AJBR2014.0755

[6] Horowitz, P. and Bowman, S. (1987) “Reversible thermal denaturation of immobilized rhodanese,” Journal of Biological Chemistry. 262. (12) 5587–5591.

[7] Itakorode, B. O., Okonji, R. E., Adedeji, O., Torimiro, N., Onwudiegwu, C., & Oluwaseyi, A. (2019). Studies on some physicochemical properties of Rhodanese synthesized by Bacillus cereus isolated from the effluents of iron and steel smelting industry. Afr J Biochem Res, 13(1), 1-8.

[8] Ogata, K., Dai, X., and Volini, M. (1989) Bovine Mitochondrial Rhodanese is a Phosphoprotein J. Biol. Chem. 264,2718-2725

[9] Palmer. T. and Bonner, P.L (2011) Enzymes: Biochemistry, Biotechnology and Clinical Chemistry 2nd Ed. Woodhead Publishing Limited, Philadelphia New Delhi

[10] Ploegman, J. H., Drent, G. and Kalk, “K. H. (1878) The covalent and tertiary structure of bovine liver rhodanese,” Nature. 273, (5658) 124–129.

[11] Shuler, M. L., and Kargi, F. (2002). Bioprocess enginnering: Basic concepts (2nd ed.). Hoboken, NJ: Prentice Hall PTR

[12] Tayefi-Nasrabadi, H. and Rahmani, R. (2012) Partial Purification and Characterization of Rhodanese from Rainbow Trout (Oncorhynchus mykiss) Liver. The ScientificWorld Journal. 2012 1-5. doi:10.1100/2012/648085

[13] Westley, J. (1973) Rhodanese.. Adv. Enzyrnol. Relat. Areas Mol. Biol. 3 9 , 327-368

[14] Whitaker, J. R. (1994). Principles of Enzymology for the Food Sciences. New York, Marcel Dekker, INC. New York.

[15] Wodu, E., Frank-Oputu, A., Lucky-Ben, K., Oweifa, M., & Appah, I. O. (2021). Studies on some Physiochemical Properties of Crude Extracts of Rhodanese from Liver and Kidney of an Adult Ram. Glob Acad J Agri Biosci, 3(3) 1-5.

[16] Zubay, G., Parson, W.W. and Vance, D.E. (1995) Principles of Biochemistry. Win. C. Brown USA

How to cite this paper

Ebizimor Wodu, Ayibaene Frank-Oputu "Temperature and pH Stability of Crude Rhodanese Enzyme Extracted from Synodontis schall" Iconic Research And Engineering Journals Volume 5 Issue 12 2022 Page 23-26
Ebizimor Wodu, Ayibaene Frank-Oputu "Temperature and pH Stability of Crude Rhodanese Enzyme Extracted from Synodontis schall" Iconic Research And Engineering Journals, vol. 5, no. 12, Jun. 2022
Ebizimor Wodu, Ayibaene Frank-Oputu (2022). Temperature and pH Stability of Crude Rhodanese Enzyme Extracted from Synodontis schall. Iconic Research And Engineering Journals, 5(12).
Ebizimor Wodu, Ayibaene Frank-Oputu "Temperature and pH Stability of Crude Rhodanese Enzyme Extracted from Synodontis schall" Iconic Research And Engineering Journals, vol. 5, no. 12, Jun. 2022.
@article{1703484,
      author = {Ebizimor Wodu, Ayibaene Frank-Oputu},
      title = {Temperature and pH Stability of Crude Rhodanese Enzyme Extracted from Synodontis schall},
      journal = {Iconic Research And Engineering Journals},
      year = {2022},
      volume = {5},
      number = {12},
      pages = {23-26},
      issn = {2456-8880},
      url = {https://www.irejournals.com/formatedpaper/1703484.pdf},
      abstract = {This research investigates the effect of temperature and pH on the stability of the enzyme extracted from the gills and liver of Synodontis schall. Rhodanese activity was assayed by measuring the amount of product formed in ?moles at 37?C and pH 8.2 per minute. The pH stability was done with pH 5.5 ? 10.0, while 20 - 60?Cwas used to determine temperature stability. The results showed that gills rhodanese was stable within the range of pH 7.5 to 9.0, while the liver enzyme was stable within the pH range of 7.5 to 9.5. Both enzymes were stable at 30 and 400C. At 500C also the liver rhodanses was stable after incubating for 40mins, but lose 60% of its activity as the time of incubation increased. Rhodanese from the gills was not stable at higher temperatures as it loses more than 60% of its initial activity upon incubation for 10mins.},
      month = {June},
  }