Share This Article:

Calcium Salts Enhance Activity and Azo Dye Decolourisation Capacity of Crude Peroxidase from Armoracia rusticana

Abstract Full-Text HTML Download Download as PDF (Size:221KB) PP. 212-218
DOI: 10.4236/ajps.2014.52028    3,131 Downloads   4,186 Views   Citations

ABSTRACT

Armoracia rusticana is the commercial source of the enzyme Horseradish Peroxidase (HRP). Calcium ions play an important role in the functional conformation of HRP. The present study assesses the effect of three calcium salts viz., calcium chloride (CaCl2), calcium nitrate [Ca(NO3)2] and calcium sulphate (CaSO4) on the guaiacol activity of crude peroxidase extracted from the shoots and roots of in vitro grown plantlets of A. rusticana and their growth medium. The highest activity was observed in the shoot extracts of 25 mM CaCl2 treated plantlets (1.92 U/mL) and the root extracts of 25 mM Ca(NO3)2 supplemented plantlets (2.84 U/mL). The crude peroxidase activity of the medium containing 25 mM CaCl2 supplement was highest (0.13 U/mL). The capacity of the shoot and root extracts to decolourise a 10 ppm solution of methyl orange over 48 hours, was also tested. The decolourisation capacity was highest in the shoot extracts from CaCl2 treated plantlets (49.32%) and root extracts from Ca(NO3)2 treated plantlets (29.72%) respectively. Hence, the addition of calcium salts to growth medium enhances both peroxidase activity and decolourisation capacity of crude extracts of A. rusticana plantlets. These findings are of significance in enzymatic treatment for decolourisation of effluents containing dyestuffs.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

M. Ambatkar and U. Mukundan, "Calcium Salts Enhance Activity and Azo Dye Decolourisation Capacity of Crude Peroxidase from Armoracia rusticana," American Journal of Plant Sciences, Vol. 5 No. 2, 2014, pp. 212-218. doi: 10.4236/ajps.2014.52028.

References

[1] N. C. Veitch, “Horseradish Peroxidase: A Modern View of a Classical Enzyme,” Phytochemistry, Vol. 65, No. 3, 2004, pp. 249-259.
http://dx.doi.org/10.1016/j.phytochem.2003.10.022
[2] A. Vianello, M. Zancani, G. Nagy and F. Macri, “Guaiacol Peroxidase Associated to Soybean Root Plasma Membranes Oxidizes Ascorbate,” Journal of Plant Physiology, Vol. 150, No. 5, 1997, pp. 573-577.
http://dx.doi.org/10.1016/S0176-1617(97)80321-5
[3] G. Nie and S. D. Aust, “Effect of Calcium on the Reversible Thermal Inactivation of Lignin Peroxidase,” Archives of Biochemistry and Biophysics, Vol. 337, No. 2, 1997, pp. 225-231. http://dx.doi.org/10.1006/abbi.1996.9770
[4] G. Nie and S. D. Aust, “Spectral Changes of Lignin Peroxidase during Reversible Inactivation,” Biochemistry, Vol. 36, No. 17, 1997, pp. 5113-5119.
http://dx.doi.org/10.1021/bi962583o
[5] B. Alberts, A. Johnson, J. Lewis, M. Raff, K. Roberts and P. Walters, “Molecular Biology of the Cell,” 5th Edition, Garland Science, New York, 2007.
[6] J. Sambrook and D. W. Russell, “Molecular Cloning, A Laboratory Manual Vol. 1,” Cold Spring Harbor Laboratory Press, New York, 2001.
[7] S. C. Fry, “Polymer-Bound Phenols as Natural Substrates of Peroxidases,” In: H. Greppin, C. Penel and Th. Gaspar, Eds., Molecular and Physiological Aspects of Plant Peroxidases, University of Geneva, Geneva, 1986, pp. 169-182.
[8] L. Sticher, C. Penel and H. Greppin, “Calcium Requirement for the Secretion of Peroxidases by Plant Cell Suspensions,” Journal of Cell Science, Vol. 48, No. 1, 1981, pp. 345-353.
[9] S. Kwak, S. Kim, I. Park and J. Liu, “Enhancement of Peroxidase Activity by Stress-Related Chemicals in Sweet Potato,” Phytochemistry, Vol. 43, No. 3, 1996, pp. 565-568. http://dx.doi.org/10.1016/0031-9422(96)00315-9
[10] J. H. Dodd and L. W. Roberts, “Experiments in Plant Tissue Culture,” Cambridge University Press, Cambridge, 1985.
[11] O. H. Lowry, N. J. Rosenbrough, A. L. Lewis-Farr and R. Randall, “Protein Measurements with Folin Phenol Reagent,” Journal of Biological Chemistry, Vol. 193, No. 1, 1951, pp. 265-275.
[12] Y. H. Kim and J. Y. Yoo, “Peroxidases Production form Carrot Hairy Root Cell Culture,” Enzyme and Microbial Technology, Vol. 18, No. 7, 1996, pp. 531-535.
http://dx.doi.org/10.1016/0141-0229(95)00168-9
[13] M. A. Habib, I. M. I. Ismail, A. J. Mahmood and M. R. Ullah, “Decolourization and Mineralization of Brilliant Golden Yellow (BGY) by Fenton and Photo-Fenton Processes,” African Journal of Pure and Applied Chemistry, Vol. 6, No. 14, 2012, pp. 153-158.
[14] P. K. Hepler, “Calcium: A Central Regulator of Plant Growth and Development,” The Plant Cell, Vol. 17, No. 8, 2005, pp. 2142-2155.
http://dx.doi.org/10.1105/tpc.105.032508
[15] G. W. Zhang, Z. Liu, J. Zhou and Y. L. Zhu, “Effect of Ca(NO3)2 Stress on Oxidative Damage, Antioxidant Enzyme Activities and Polyamine Contents in Roots of Grafted and Non-Grafted Tomato Plants,” Plant Growth Regulation, Vol. 56, No. 1, 2008, pp. 7-19.
http://dx.doi.org/10.1007/s10725-008-9281-8
[16] H. Xu, X. Sun, X. Yang, Q. Shi and X. Wang, “Physiological Responses to Nitrate Stress of Transgenic Tobacco Plants Harbouring the Cucumber Mitogen-Activated Protein Kinase Gene,” Turkish Journal of Botany, Vol. 37, No. 1, 2013, pp. 130-138.
[17] S. A. Abo-Farah, “Comparative Study of Oxidation of Some Azo Dyes by Different Advanced Oxidation Processes: Fenton, Fenton-Like, Photo-Fenton and Photo-Fenton-Like,” American Journal of Science, Vol. 6, No. 10, 2010, pp. 128-142.
[18] M. Stanisavljevic and L. Nedic, “Removal of Phenol from Industrial Wastewaters by Horseradish (Cochlearia armoracia L.),” Working and Living Environmental Protection, Vol. 2, No. 4, 2004, pp. 345-349.
[19] V. L. Maddhinni, H. B. Vurimindi and A. Yerramilli, “Degradation of Azo Dye with Horseradish Peroxidase (HRP),” Journal of the Indian Institute of Science, Vol. 86, No. 5, 2006, pp. 507-514.
[20] I. Morishima, M. Kurono and Y. Shiro, “Presence of Endogenous Calcium Ion in Horseradish Peroxidase,” The Journal of Biological Chemistry, Vol. 261, No. 20, 1986, pp. 9391-9399.
[21] C. Penel, “The Role of Calcium in the Control of Peroxidase Activity,” In: H. Greppin, C. Penel and Th. Gaspar, Eds., Molecular and Physiological Aspects of Plant Peroxidases, University of Geneva, Geneva, 1986, pp. 155-164.
[22] A. Oscar, V. Moreno, R. Vazquez-Duhalt and J. L. Ochoa, “Peroxidase Activity in Calluses and Cell Suspension Cultures of Radish Raphanus sativus var. Cherry Bell,” Plant Cell, Tissue and Organ Culture, Vol. 18, No. 3, 1989, pp. 321-327.
http://dx.doi.org/10.1007/BF00043401
[23] M. Laberge, Q. Huang, R. Schwietzer-Stenner and J. Fidy, “The Endogenous Calcium Ions of Horseradish Peroxides C Are Required to Maintain the Functional Nonplanarity of the Heme,” Biophysical Journal, Vol. 84, No. 4, 2003, pp. 2542-2552.
http://dx.doi.org/10.1016/S0006-3495(03)75059-0
[24] C. Indiani, B. D. Howes, A. Feis and G. Smulevich, “Calcium Depletion of Horseradish Peroxidase Generates a Quantum Mechanical Mixed-Spinheme State,” In: J. Greve, G. J. Puppels and C. Otto, Eds., Spectroscopy of Biological Molecules: New Directions, Springer, Dordrecht, 1999, pp. 145-146.
http://dx.doi.org/10.1007/978-94-011-4479-7_62
[25] Y. Shiro, M. Kurono and I. Morishima, “Presence of Endogenous Calcium Ions and Its Functional and Structural Regulation in Horseradish Peroxidase,” The Journal of Biological Chemistry, Vol. 261, No. 20, 1986, pp. 9382-9390.

  
comments powered by Disqus

Copyright © 2018 by authors and Scientific Research Publishing Inc.

Creative Commons License

This work and the related PDF file are licensed under a Creative Commons Attribution 4.0 International License.