Volume 2, Issue 2, December 2018, Page: 52-59
Structure, Function and Applications of a Classic Enzyme: Horseradish Peroxidase
Hameed Akbar, Laboratory of Cellular Dynamics, School of Life Science, University of Science and Technology of China, Hefei, China
Divine Mensah Sedzro, Laboratory of Cellular Dynamics, School of Life Science, University of Science and Technology of China, Hefei, China
Mazhar Khan, Molecular & Cytogenetics Lab, School of Life Science, University of Science and Technology of China, Hefei, P R China
Sm Faysal Bellah, Laboratory of Cellular Dynamics, School of Life Science, University of Science and Technology of China, Hefei, China; Department of Pharmacy, Manarat International University, Dhaka, Bangladesh
S M Saker Billah, Department of Chemistry, Govt. M. M. University College, Jessore, Bangladesh
Received: Oct. 14, 2018;       Accepted: Oct. 29, 2018;       Published: Nov. 27, 2018
DOI: 10.11648/j.jcebe.20180202.13      View  179      Downloads  46
Abstract
An oxidation-reduction catalyzing enzyme i.e. peroxidases that are produced by numerous plants and microorganism are widely known in today’s world. This enzyme can catalyze peroxide based reactions. Novel types of aromatic polymers may result from the oxidative polymerization of aromatic amines and phenols by horseradish Peroxidase (HRP) present in water or water-soluble organic solvents. Besides, playing a potential role by the peroxidases in the soil detoxification, HRP, turnip and soybean peroxidases have also shown their significance in the bioremediation of cresols, phenols and chlorinated phenols contaminated water. Other types like manganese peroxidase (MnP) and Lignin Peroxidase (LiP) are of important use in paper industry for performing bio-bleaching and bio-pulping. These enzymes can also oxidatively breakdown the synthetic azo dyes. One of the major use of peroxidases are in analytical systems where peroxidase based biosensors are used for organic hydroperoxide and hydrogen peroxide determination. On the other hand, if co-immobilized with H2O2–producing enzyme, it can be used for determination of range of compounds e.g. alcohols, choline, glucose and glutamate. Furthermore, peroxidases are simple and trustworthy way of detecting pathogens, toxins and antigens in various analytes by labeling a pre applied antibody like in ELISA (enzyme immuno sorbent assay) and quantification of chemicals like glucose, lactose, uric acid and cholesterol that are its practical analytical applications in diagnostic kits.
Keywords
Horseradish Peroxidase, Biochemical Assays, Bioremediation, Bio-Bleaching, Bio-Pulping
To cite this article
Hameed Akbar, Divine Mensah Sedzro, Mazhar Khan, Sm Faysal Bellah, S M Saker Billah, Structure, Function and Applications of a Classic Enzyme: Horseradish Peroxidase, Journal of Chemical, Environmental and Biological Engineering. Vol. 2, No. 2, 2018, pp. 52-59. doi: 10.11648/j.jcebe.20180202.13
Copyright
Copyright © 2018 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Reference
[1]
Wakamatsu, K., & Takahama, U. (1993). Changes in peroxidase activity and inperoxidase isozymes in carrot callus. Physiology of Plant, 68, 167–171.
[2]
Biles, C. L., &Martyn, R. D. (1993). Peroxidase, polyphenol oxidase and shikimate dehydrogenase isozymes in relation to the tissue type, maturity and pathogen induction of watermelon seedlings. Plant Physiology and Biochemistry, 31,499–506.
[3]
Wong, D. W. S. (1995). Food enzymes, structure and mechanism. New York: Chapman and Hall. pp. 327–332.
[4]
Chung, K. T., Kirkovsky, L., Kirkovsky, A., & Purcell, W. P. (1997). Review of mutagenicity of monocylic aromatic amines: Quantitative structure activity relationships. Mutation Research, 387, 1–16.
[5]
Mantha, R., Biswas, N., Taylor, K. E., & Bewtra, J. K. (2002). Removal of nitroaromatics from synthetic waste water using two-step zero valent ion reduction and peroxidase catalyzed oxidative polymerization. Water Environment Research, 74,280–287.
[6]
Lin, Z. F., Chen, L. H., & Zhang, W. Q. (1996). Peroxidase from I. Cairica (L) SW. Isolation, purification and some properties. Process of Biochemistry, 5, 443–448.
[7]
Agostini, E., Hernandez-Ruiz, J., Arnao, M. B., Milrand, S. R., Tigier, H. A., & Acosta, M.(2002). A peroxidase isoenzyme secreted by turnip (Brassica napus) hairy-root culture inactivation by hydrogen peroxide and application in diagnostic kits. Biotechnology and Applied Biochemistry, 35, 1–7.
[8]
Kim, Y. H., &Yoo, J. Y. (1996). Peroxidase production from carrot hairy root cell culture. Enzyme Microbiology and Technology, 18, 531–535.
[9]
Egorov, A. M., Reshetnikova, I. A., Fechina, V. A., &Gazaryan, I. G. (1995). Comparative studies of plant and fungal peroxidases. Annal of the New York Academic Science, 750, 469–472.
[10]
Krell, H. W. (1991). Peroxidase: An important enzyme for diagnostic test kits. In J. Loburzewski, H. Greppin, C. Penel, & T. Gaspar (Eds.), Biochemical, molecular and physiological aspects of plant peroxidases (pp. 469–478). Lublind, Poland and Geneva, Switzerland: University of Maria Curie-Sklodowska and University of Geneva.
[11]
Welinder, K. G., 1976. Covalent structure of the glycoprotein horseradish peroxidase. FEBS Lett. 72, 19–23.
[12]
Yang, B. Y., Gray, J. S. S., Montgomery, R., 1996. The glycans of horseradish peroxidase. Carbohydrate Res. 287, 203–212.
[13]
Gajhede, M., Schuller, D. J., Henriksen, A., Smith, A. T., Poulos, T. L., 1997. Crystal structure of horseradish peroxidase C at 2.15angstrom resolution. Nature Struct. Biol. 4, 1032–1038.
[14]
Welinder, K. G., Gajhede, M., 1993. Structure and evolution of peroxidases. Welinder, K. G., Rasmussen, S. K., Penel, C., Greppin, H. (Eds.), Plant Peroxidases: Biochemistry and Physiology. University of Geneva, Geneva, pp. 35–42.
[15]
Smith, A. T., Veitch, N. C., 1998. Substrate binding and catalysis inheme peroxidases. Curr. Opin. Chem. Biol. 2, 269–278.
[16]
Mittler, R., 2002. Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci. 7, 405–410.
[17]
Shigeoka, S., Ishikawa, T., Tamoi, M., Miyagawa, Y., Takeda, T., Yabuta, Y., Yoshimura, K., 2002. Regulation and function of ascorbate peroxidase isoenzymes. J. Exp. Biol. 53, 1305–1319.
[18]
Berglund, G. I., Carlsson, G. H., Smith, A. T., Szo¨ ke, H., Henriksen, A., Hajdu, J., 2002. The catalytic pathway of horseradish peroxidaseat high resolution. Nature 417, 463–468.
[19]
Henriksen, A., Smith, A. T., Gajhede, M., 1999. The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates. J. Biol. Chem. 274, 35005–35011.
[20]
Ortiz de Montellano, P. R., 1992. Catalytic sites of hemoprotein peroxidases. Annu. Rev. Pharmacol. Toxicol. 32, 89–107.
[21]
Newmyer, S. L., Ortiz de Montellano, P. R., 1995. Horseradish peroxidaseHis-42Ala, His-42Val, and Phe-41Ala mutants. Histidine catalysis and control of substrate access to the heme iron. J. Biol. Chem. 270, 19430–19438.
[22]
Ozaki, S., Ortiz de Montellano, P. R., 1995. Molecular engineering of horseradish peroxidase; thioether sulfoxidation and styrene epoxidation by Phe-41 leucine and threonine mutants. J. Am. Chem. Soc. 117, 7056–7064.
[23]
Henriksen, A., Smith, A. T., Gajhede, M., 1999. The structures of the horse radish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates. J. Biol. Chem. 274, 35005–35011.
[24]
Veitch, N. C., Smith, A. T., 2001. Horseradish peroxidase. Adv. Inorg. Chem. 51, 107–162.
[25]
Jia, J. B., Wang, B. Q., Wu, A. G., Cheng, G. J., Li, Z., & Dong, S. J. (2002). A method to construct a third generation horseradish peroxidase biosensor; self-assembling gold nanoparticles to three-dimensional sol-gel network. Analytical Chemistry, 74, 2217–2223.
[26]
Munteanu, F. D., Lindgren, A., Emneus, J., Gorton, L., Ruzgas, T., Csoregi, E., et al.(1998). Bioelectrochemical monitoring of phenol and aromatic amines in flow injection using novel plant peroxidases. Analytical Chemistry, 70, 2596–2600.
[27]
Sharma, A. K., Sehgal, N., & Kumar, A. (2002). A quick and simple biostrip techniquefor detection of lactose. Biotechnology Letters, 24, 1737–1739.
[28]
Hirany, S., Li, D., & Jialal, I. (1997). A more valid measurement of low density lipoprotein cholesterol in diabetic patients. American Journal of Medical, 102,48–53.
[29]
Ragland, B. D., Kourad, R. J., Chaffin, C., Robinson, C. A., & Hardy, R. W. (2000). Evaluation of homogenous direct LDL-cholesterol assay in diabetic patient: Effect of glycemic control. Clinical Chemistry, 46, 1848–1851.
[30]
Malik, V., & Pundir, C. S. (2002). Determination of total cholesterol in serum by cholesterol esterase and cholesterol oxidase immobilized and co-immobilized on to arylamino glass. Biotechnology and Applied Biochemistry, 35, 191–197.
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