Journal of Chemical, Environmental and Biological Engineering

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Structure, Function and Applications of a Classic Enzyme: Horseradish Peroxidase

Received: Oct. 14, 2018    Accepted: Oct. 29, 2018    Published: Nov. 27, 2018
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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.

DOI 10.11648/j.jcebe.20180202.13
Published in Journal of Chemical, Environmental and Biological Engineering ( Volume 2, Issue 2, December 2018 )
Page(s) 52-59
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Horseradish Peroxidase, Biochemical Assays, Bioremediation, Bio-Bleaching, Bio-Pulping

References
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[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.
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  • APA Style

    Hameed Akbar, Divine Mensah Sedzro, Mazhar Khan, Sm Faysal Bellah, S M Saker Billah. (2018). Structure, Function and Applications of a Classic Enzyme: Horseradish Peroxidase. Journal of Chemical, Environmental and Biological Engineering, 2(2), 52-59. https://doi.org/10.11648/j.jcebe.20180202.13

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    ACS Style

    Hameed Akbar; Divine Mensah Sedzro; Mazhar Khan; Sm Faysal Bellah; S M Saker Billah. Structure, Function and Applications of a Classic Enzyme: Horseradish Peroxidase. J. Chem. Environ. Biol. Eng. 2018, 2(2), 52-59. doi: 10.11648/j.jcebe.20180202.13

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    AMA Style

    Hameed Akbar, Divine Mensah Sedzro, Mazhar Khan, Sm Faysal Bellah, S M Saker Billah. Structure, Function and Applications of a Classic Enzyme: Horseradish Peroxidase. J Chem Environ Biol Eng. 2018;2(2):52-59. doi: 10.11648/j.jcebe.20180202.13

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  • @article{10.11648/j.jcebe.20180202.13,
      author = {Hameed Akbar and Divine Mensah Sedzro and Mazhar Khan and Sm Faysal Bellah and S M Saker Billah},
      title = {Structure, Function and Applications of a Classic Enzyme: Horseradish Peroxidase},
      journal = {Journal of Chemical, Environmental and Biological Engineering},
      volume = {2},
      number = {2},
      pages = {52-59},
      doi = {10.11648/j.jcebe.20180202.13},
      url = {https://doi.org/10.11648/j.jcebe.20180202.13},
      eprint = {https://download.sciencepg.com/pdf/10.11648.j.jcebe.20180202.13},
      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.},
     year = {2018}
    }
    

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  • TY  - JOUR
    T1  - Structure, Function and Applications of a Classic Enzyme: Horseradish Peroxidase
    AU  - Hameed Akbar
    AU  - Divine Mensah Sedzro
    AU  - Mazhar Khan
    AU  - Sm Faysal Bellah
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    T2  - Journal of Chemical, Environmental and Biological Engineering
    JF  - Journal of Chemical, Environmental and Biological Engineering
    JO  - Journal of Chemical, Environmental and Biological Engineering
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    PB  - Science Publishing Group
    SN  - 2640-267X
    UR  - https://doi.org/10.11648/j.jcebe.20180202.13
    AB  - 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.
    VL  - 2
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Author Information
  • Laboratory of Cellular Dynamics, School of Life Science, University of Science and Technology of China, Hefei, China

  • Laboratory of Cellular Dynamics, School of Life Science, University of Science and Technology of China, Hefei, China

  • Molecular & Cytogenetics Lab, School of Life Science, University of Science and Technology of China, Hefei, P R China

  • 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

  • Department of Chemistry, Govt. M. M. University College, Jessore, Bangladesh

  • Section