A Review on Recognition of Various Peroxidases

Xin Li; Fangdi Cong; Shulin Zhang; Dajuan Zhang; Xinxin Wang

doi:doi:10.11648/j.ijbc.20200501.13

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A Review on Recognition of Various Peroxidases

Xin Li, Fangdi Cong, Shulin Zhang, Dajuan Zhang, Xinxin Wang

Published in International Journal of Bioorganic Chemistry (Volume 5, Issue 1)

Received: 5 December 2019 Accepted: 20 December 2019 Published: 8 January 2020

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Abstract

Peroxidases, widespread in the biological world, are a kind of oxidoreductases important in biological antioxidant defense systems. For great potential value of them in physiology, biochemistry and treatment of industrial pollutants, etc., they receive extraordinary attention, and also a large number of peroxidases have been found and studied on the nature and catalytic properties of them to date. Especially, horseradish peroxidase is first found and given more researches on the protein structure, catalytic mechanism and practical applications, and even modified by gene engineering and protein engineering to improve its catalytic performance. In addition, also there are numerous peroxidases that are derived from various sources or used for catalytic oxidation of different substrates, which have many differences from horseradish peroxidase in amino acid composition, active site structure, catalytic characteristics and corresponding applications. To better study and selectively employ peroxidases as biocatalysts, it is critical to comprehensively recognize various peroxidases, so as to present a reference for the in-depth and accurate studies on them in the future. In this paper, various peroxidases usually focused by enzymologists are reviewed for better mastering the completed research work on them, understanding the main interests in them, and knowing the advantages and disadvantages of them. Moreover, the research aspects that hereafter may be focused on are prospected.

Published in	International Journal of Bioorganic Chemistry (Volume 5, Issue 1)
DOI	10.11648/j.ijbc.20200501.13
Page(s)	10-14
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), 2020. Published by Science Publishing Group

Keywords

Peroxidase, Catalysis, Review, Application

References

[1]	Poulos T L, Kraut J (1980) The stereochemistry of peroxidase catalysis. J Biol Chem 255 (17), 8199-205.
[2]	Saunders B C, Holmes-Siedle A G, Stark B P (1964) The properties and uses of a versatile enzyme and of some related catalysts. In: Peroxidase. London: Butterworths. p. 214–52.
[3]	Planche L A (1809) Chemical account of the angustura of commerce, wherein the means are pointed out of ascertaining the true kind. Med Phys J 22 (126), 144-149.
[4]	Berglund G I, Carlsson G H, Smith A T, Szöke H, Henriksen A, Hajdu J (2002) The catalytic pathway of horseradish peroxidase at high resolution. Nature 417 (6887), 463-468.
[5]	Rook G A (1981) Chromosomes for the enzyme-linked immunosorbent assay (elisa) using horse-radish peroxidase. Leprosy rev 52 (3), 281-283.
[6]	Seifu E, Buys EM, Donkin E F (2005) Significance of the lactoperoxidase system in the dairy industry and its potential applications: a review. Trends Food Sci Tech 16 (4), 0-154.
[7]	Dama M, Steiner M, Lieshout R V (2016) Thyroid peroxidase autoantibodies and perinatal depression risk: a systematic review. J Affect Disorders S0165032715312076.
[8]	Lei X G, Cheng W H, Mcclung J P (2007) Metabolic regulation and function of glutathione peroxidase-1. Annu Rev Nutr 27 (1), 41-61.
[9]	Smulevich G, Jakopitsch C, Droghetti E, Obinger C (2006) Probing the structure and bifunctionality of catalase-peroxidase (katg). J Inorg Biochem 100 (4), 568-585.
[10]	Veeger C (2002) Does p450-type catalysis proceed through a peroxo-iron intermediate? a review of studies with microperoxidase. J Inorg Biochem 91 (1), 35-45.
[11]	Huystee R B V, Cairns W L (1980) Appraisal of studies on induction of peroxidase and associated porphyrin metabolism. Bot Rev 46 (4), 429-446.
[12]	Burnette F S (2006) Peroxidase and its relationship to food flavor and quality: a review. J Food Sci 42 (1), 1-6.
[13]	Bindoli A, Fukuto J M, Forman H J (2008) Thiol chemistry in peroxidase catalysis and redox signaling. Antioxid Redox Sig 10 (9), 1549-1564.
[14]	Mcdonagh A F, Vreman H J, Wong R J, Stevenson D K (2009) Photoisomers: obfuscating factors in clinical peroxidase measurements of unbound bilirubin?. Pediatrics 123 (1), 67-76.
[15]	Mo D (2018) Research on the interaction mechanism of Laccase and Horseradish peroxidase with phenolic pollutants based on molecular docking. Hunan University.
[16]	Junker K, Gitsov I, Quade N, Walde P (2013) Preparation of aqueous polyaniline-vesicle suspensions with class III peroxidases. Comparison between horseradish peroxidase isoenzyme C and soybean peroxidase. Chem Paper, 67 (8), 1028-1047.
[17]	Delincée H, Radola B J. (1997) Thin-layer isoelectric focusing on Sephadex layers of horseradish peroxidase. BBA, 200 (2), 404-407.
[18]	Gajhede M, Schuller D J, Henriksen A, Smith A T, Poulos T L. (1997) Crystal structure of horseradish peroxidase C at 2.15 A resolution. Nature struct biol, 4 (12): 1032-1038.
[19]	Derat E, Shaik S, Rovira C, Vidossich P, Alfonso-Prieto M (2007) The effect of a water molecule on the mechanism of formation of compound 0 in Horseradish peroxidase. J Am Chem Soc 129 (20), 6346-6347.
[20]	Veitch N C (2004) Horseradish peroxidase: a modern view of a classic enzyme. Phytochem (Amsterdam) 65 (3), 249-259.
[21]	Vineh M B, Saboury A A, Poostchi A A, Rashid A M, Parivar K (2018) Stability and activity improvement of horseradish peroxidase by covalent immobilization on functionalized reduced graphene oxide and biodegradation of high phenol concentration. Inter J Biol Macromol, 106, 1314-1322.
[22]	Ó’Fágáin C (2003) Enzyme stabilization-recent experimental progress. Enzyme Microb Tech 33 (2), 137-149.
[23]	Ruzgas T, Csöregi E, Emnéus J, Gorton L, Marko-Varga G (1996) Peroxidase-modified electrodes: Fundamentals and application. Anal Chim Acta 330 (2-3), 123-138.
[24]	Teraoka J, Ogura T, Kitagawa T (1982) Resonance Raman spectra of the reaction intermediates of horseradish peroxidase catalysis. J Am Chem Soc 104 (25), 7354-7356.
[25]	Elena-Florentina G, Gabriela C, Renato F (2018) Development of horseradish peroxidase/layered double hydroxide hybrid catalysis for phenol degradation. Res Chem Intermediat 44 (12), 7731–7752.
[26]	Na S Y, Lee Y (2017) Elimination of trace organic contaminants during enhanced wastewater treatment with horseradish peroxidase/hydrogen peroxide (HRP/H₂O₂) catalytic process. Catal Today 282, 86-94.
[27]	Izawa H, Dote Y, Okuda N, Sumita M, Ifuku S, Morimoto M, Saimoto H (2017) Wood-mimetic skins prepared using horseradish peroxidase catalysis to induce surface wrinkling of chitosan film upon drying. Carbohyd Polym 173, 519-525.
[28]	Yang S Y, Li L Q, Chen Q, Zhuo W, Liu L. Lu L M (2018) Cloning and expression pattern analysis of Tobacco peroxidase gene NtPOD1 in nicotiana tabacum. Acta Agr Boreali-Sinica 33 (03), 110-116.
[29]	Gundinger T, Spadiut O (2017) A comparative approach to recombinantly produce the plant enzyme horseradish peroxidase in Escherichia coli. J Biotechnol 248, 15-24.
[30]	Zhang L H, Zhi L F, Jiang Y C, Hu M C, Li S N (2007) Chloroperoxidase stabilization technology and its application. Chem Life (04), 65-67.
[31]	Bai C H, Jiang Y C, Hu M C, Li S, Zhai Q (2009) Improvement of chloroperoxidase catalytic activities by chitosan and thioglycolic acid. Catal Lett 129 (3-4), 457-461.
[32]	Zhang L H. (2014) Progress in Study and Application of Chloroperoxidase. J Shanxi Datong Univ (Natural Science Edition), (2), 42-47.
[33]	Chen Y, Lin K, Chen D, Wang K, Zhou W, Wu Y, Huang X (2018) Formation of environmentally relevant polyhalogenated carbazoles from chloroperoxidase-catalyzed halogenation of carbazole. Environ Pollut 232, 264-273.
[34]	Lu J, Jiang Y C (2018) Research on the catalytic degradation process of p-aminobenzenesulfonic acid by chloroperoxidase. J Shaanxi Univ Sci Technol 36 (01), 34-39.
[35]	Corbett M D, Chipko B R (1979) Peroxide oxidation of indole to oxindole by chloroperoxidase catalysis. Biochem J 183 (2), 269-276.
[36]	Thiel D, Blume F, Jäger C, Deska J (2018) Chloroperoxidase-catalyzed achmatowicz rearrangements. Eur J Org Chem 2018 (20-21), 2717-2725.
[37]	Dembitsky V M. (2003) Oxidation, Epoxidation and sulfoxidation reactions catalyzed by haloperoxidases. Chem Inform 34 (40), 4701-4720.
[38]	Liu J Z, Yang H Y, Zhao J L, Liping W, Liangnian J (1998) A study on axial ligands of model enzyme to activize catalase a new method of enhancement natural enzyme activity. Actaentiarum Naturalium Universitatis Sunyatseni 37 (2), 125-127.
[39]	Yin V, Mian S H, Konermann L (2019) Lysine carbonylation is a previously unrecognized contributor to peroxidase activation of cytochrome c by chloramine-T. Chem Sci 10 (8), 2349-2359.
[40]	Payne T M, Yee E F, Dzikovski B, Crane B R (2016) Constraints on the radical cation center of cytochrome c peroxidase for electron transfer from cytochrome c. Biochem 55 (34), 4807-4822.
[41]	Yin V, Shaw G S, Konermann L (2017) Cytochrome c as a peroxidase: activation of the pre-catalytic native state by H₂O₂-induced covalent modifications. J Am Chem Soc 139 (44), 15701-15709.
[42]	Zhang J, Wang S, Meng F J, YanY J, Wang B, Guan Z Y (2019) Advances in research on the role of glutathione peroxidase in tumors. Chinese J Cancer 38 (6), 282-287.
[43]	Yu Y, Wei J Y (2013) Glutathione peroxidase and its synthesis mechanism. Acta Bioph Sin 29 (10), 724-737.
[44]	Zhou M, Chen Y (1985) Glutathione peroxidase. Chem Life (4), 17-18.
[45]	Ilham, Fotedar R, Munilkumar S (2016) Effects of organic selenium supplementation on growth, glutathione peroxidase activity and histopathology in juvenile barramundi (Lates calcarifer Bloch 1970) fed high lupin meal-based diets. Aquaculture 457, 15-23.
[46]	Wang H K (2004) Molecular clone of cDNA encoding lignin peroxidase and manganese peroxidase from Phanerochaete chrysosporium and expression in Pichia methanolica. Tianjin Univ Sci Technol.
[47]	Zhang X, Tian X X, Dong W F, Wang R M, Pan H C (2019) Molecular cloning, antibody prepation and expression analysis of ascorbate peroxidase in hydra sinensis. Acta Hydrobiol Sin 43 (02), 77-86.
[48]	Qiao F, Geng G G, Zeng Y, Jin L, Xie H C (2019) Molecular cloning and expression patterns of LcAPX from Lycium chinense [J]. J China Agr Univer 24 (04), 69-77.
[49]	Smulevich G, Jakopitsch C, Droghetti E, Obinger C (2006). Probing the structure and bifunctionality of catalase-peroxidase (katg). J Inorg Biochem 100 (4), 568-585.
[50]	Li G, Fan A, Peng G, Keyhani N O, Xin J, Cao Y, Xia Y. (2017). A bifunctional catalase-peroxidase, makatg 1, contributes to virulence of metarhizium acridum by overcoming oxidative stress on the host insect cuticle. Environ Microbiol 19 (10), 4365-4378.
[51]	Reyes Y I A, Jr F C F (2019) Dft study on the effect of proximal residues on the mycobacterium tuberculosis catalase-peroxidase (katg) heme compound i intermediate and its bonding interaction with isoniazid. Phys Chem Chem Phys 21 (30), 16515-16525.
[52]	Yan M, Luo Q, Lai C F, Li C, Liu L, Sun S J (2019) Study on purification technology of manganese peroxidase from spent mushroom compost of Pleurotus eryngii. Jiangsu Agr Sci, 47 (02): 305-309.
[53]	Deits T L, Shapiro B M (1986) Conformational control of ovoperoxidase catalysis in the sea urchin fertilization membrane. J Biol Chem 261 (26), 12159-65.
[54]	Dong S, Mao L, Luo S, Zhou L, Feng Y, Gao S (2014) Comparison of lignin peroxidase and horseradish peroxidase for catalyzing the removal of nonylphenol from water. Environ Sci Pollut Res 21 (3), 2358-2366.
[55]	Laurenti E, Ghibaudi E, Todaro G, Ferrari R P (2002) Enzymatic degradation of 2,6-dichlorophenol by horseradish peroxidase: UV–visible and mass spectrophotometric characterization of the reaction products. J Inorg Biochem 92 (1), 75-81.

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APA Style

Xin Li, Fangdi Cong, Shulin Zhang, Dajuan Zhang, Xinxin Wang. (2020). A Review on Recognition of Various Peroxidases. International Journal of Bioorganic Chemistry, 5(1), 10-14. https://doi.org/10.11648/j.ijbc.20200501.13

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ACS Style

Xin Li; Fangdi Cong; Shulin Zhang; Dajuan Zhang; Xinxin Wang. A Review on Recognition of Various Peroxidases. Int. J. Bioorg. Chem. 2020, 5(1), 10-14. doi: 10.11648/j.ijbc.20200501.13

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AMA Style

Xin Li, Fangdi Cong, Shulin Zhang, Dajuan Zhang, Xinxin Wang. A Review on Recognition of Various Peroxidases. Int J Bioorg Chem. 2020;5(1):10-14. doi: 10.11648/j.ijbc.20200501.13

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@article{10.11648/j.ijbc.20200501.13,
  author = {Xin Li and Fangdi Cong and Shulin Zhang and Dajuan Zhang and Xinxin Wang},
  title = {A Review on Recognition of Various Peroxidases},
  journal = {International Journal of Bioorganic Chemistry},
  volume = {5},
  number = {1},
  pages = {10-14},
  doi = {10.11648/j.ijbc.20200501.13},
  url = {https://doi.org/10.11648/j.ijbc.20200501.13},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijbc.20200501.13},
  abstract = {Peroxidases, widespread in the biological world, are a kind of oxidoreductases important in biological antioxidant defense systems. For great potential value of them in physiology, biochemistry and treatment of industrial pollutants, etc., they receive extraordinary attention, and also a large number of peroxidases have been found and studied on the nature and catalytic properties of them to date. Especially, horseradish peroxidase is first found and given more researches on the protein structure, catalytic mechanism and practical applications, and even modified by gene engineering and protein engineering to improve its catalytic performance. In addition, also there are numerous peroxidases that are derived from various sources or used for catalytic oxidation of different substrates, which have many differences from horseradish peroxidase in amino acid composition, active site structure, catalytic characteristics and corresponding applications. To better study and selectively employ peroxidases as biocatalysts, it is critical to comprehensively recognize various peroxidases, so as to present a reference for the in-depth and accurate studies on them in the future. In this paper, various peroxidases usually focused by enzymologists are reviewed for better mastering the completed research work on them, understanding the main interests in them, and knowing the advantages and disadvantages of them. Moreover, the research aspects that hereafter may be focused on are prospected.},
 year = {2020}
}

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TY  - JOUR
T1  - A Review on Recognition of Various Peroxidases
AU  - Xin Li
AU  - Fangdi Cong
AU  - Shulin Zhang
AU  - Dajuan Zhang
AU  - Xinxin Wang
Y1  - 2020/01/08
PY  - 2020
N1  - https://doi.org/10.11648/j.ijbc.20200501.13
DO  - 10.11648/j.ijbc.20200501.13
T2  - International Journal of Bioorganic Chemistry
JF  - International Journal of Bioorganic Chemistry
JO  - International Journal of Bioorganic Chemistry
SP  - 10
EP  - 14
PB  - Science Publishing Group
SN  - 2578-9392
UR  - https://doi.org/10.11648/j.ijbc.20200501.13
AB  - Peroxidases, widespread in the biological world, are a kind of oxidoreductases important in biological antioxidant defense systems. For great potential value of them in physiology, biochemistry and treatment of industrial pollutants, etc., they receive extraordinary attention, and also a large number of peroxidases have been found and studied on the nature and catalytic properties of them to date. Especially, horseradish peroxidase is first found and given more researches on the protein structure, catalytic mechanism and practical applications, and even modified by gene engineering and protein engineering to improve its catalytic performance. In addition, also there are numerous peroxidases that are derived from various sources or used for catalytic oxidation of different substrates, which have many differences from horseradish peroxidase in amino acid composition, active site structure, catalytic characteristics and corresponding applications. To better study and selectively employ peroxidases as biocatalysts, it is critical to comprehensively recognize various peroxidases, so as to present a reference for the in-depth and accurate studies on them in the future. In this paper, various peroxidases usually focused by enzymologists are reviewed for better mastering the completed research work on them, understanding the main interests in them, and knowing the advantages and disadvantages of them. Moreover, the research aspects that hereafter may be focused on are prospected.
VL  - 5
IS  - 1
ER  -

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Author Information

Xin Li

Tianjin Key Laboratory of Aqua-ecology and Aquaculture, College of Basic Science, Tianjin Agricultural University, Tianjin, China
Fangdi Cong

Tianjin Key Laboratory of Aqua-ecology and Aquaculture, College of Basic Science, Tianjin Agricultural University, Tianjin, China
Shulin Zhang

Tianjin Key Laboratory of Aqua-ecology and Aquaculture, College of Basic Science, Tianjin Agricultural University, Tianjin, China
Dajuan Zhang

Tianjin Key Laboratory of Aqua-ecology and Aquaculture, College of Basic Science, Tianjin Agricultural University, Tianjin, China
Xinxin Wang

Tianjin Key Laboratory of Aqua-ecology and Aquaculture, College of Basic Science, Tianjin Agricultural University, Tianjin, China

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APA Style

Xin Li, Fangdi Cong, Shulin Zhang, Dajuan Zhang, Xinxin Wang. (2020). A Review on Recognition of Various Peroxidases. International Journal of Bioorganic Chemistry, 5(1), 10-14. https://doi.org/10.11648/j.ijbc.20200501.13

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ACS Style

Xin Li; Fangdi Cong; Shulin Zhang; Dajuan Zhang; Xinxin Wang. A Review on Recognition of Various Peroxidases. Int. J. Bioorg. Chem. 2020, 5(1), 10-14. doi: 10.11648/j.ijbc.20200501.13

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AMA Style

Xin Li, Fangdi Cong, Shulin Zhang, Dajuan Zhang, Xinxin Wang. A Review on Recognition of Various Peroxidases. Int J Bioorg Chem. 2020;5(1):10-14. doi: 10.11648/j.ijbc.20200501.13

Copy | Download

@article{10.11648/j.ijbc.20200501.13,
  author = {Xin Li and Fangdi Cong and Shulin Zhang and Dajuan Zhang and Xinxin Wang},
  title = {A Review on Recognition of Various Peroxidases},
  journal = {International Journal of Bioorganic Chemistry},
  volume = {5},
  number = {1},
  pages = {10-14},
  doi = {10.11648/j.ijbc.20200501.13},
  url = {https://doi.org/10.11648/j.ijbc.20200501.13},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijbc.20200501.13},
  abstract = {Peroxidases, widespread in the biological world, are a kind of oxidoreductases important in biological antioxidant defense systems. For great potential value of them in physiology, biochemistry and treatment of industrial pollutants, etc., they receive extraordinary attention, and also a large number of peroxidases have been found and studied on the nature and catalytic properties of them to date. Especially, horseradish peroxidase is first found and given more researches on the protein structure, catalytic mechanism and practical applications, and even modified by gene engineering and protein engineering to improve its catalytic performance. In addition, also there are numerous peroxidases that are derived from various sources or used for catalytic oxidation of different substrates, which have many differences from horseradish peroxidase in amino acid composition, active site structure, catalytic characteristics and corresponding applications. To better study and selectively employ peroxidases as biocatalysts, it is critical to comprehensively recognize various peroxidases, so as to present a reference for the in-depth and accurate studies on them in the future. In this paper, various peroxidases usually focused by enzymologists are reviewed for better mastering the completed research work on them, understanding the main interests in them, and knowing the advantages and disadvantages of them. Moreover, the research aspects that hereafter may be focused on are prospected.},
 year = {2020}
}

Copy | Download

TY  - JOUR
T1  - A Review on Recognition of Various Peroxidases
AU  - Xin Li
AU  - Fangdi Cong
AU  - Shulin Zhang
AU  - Dajuan Zhang
AU  - Xinxin Wang
Y1  - 2020/01/08
PY  - 2020
N1  - https://doi.org/10.11648/j.ijbc.20200501.13
DO  - 10.11648/j.ijbc.20200501.13
T2  - International Journal of Bioorganic Chemistry
JF  - International Journal of Bioorganic Chemistry
JO  - International Journal of Bioorganic Chemistry
SP  - 10
EP  - 14
PB  - Science Publishing Group
SN  - 2578-9392
UR  - https://doi.org/10.11648/j.ijbc.20200501.13
AB  - Peroxidases, widespread in the biological world, are a kind of oxidoreductases important in biological antioxidant defense systems. For great potential value of them in physiology, biochemistry and treatment of industrial pollutants, etc., they receive extraordinary attention, and also a large number of peroxidases have been found and studied on the nature and catalytic properties of them to date. Especially, horseradish peroxidase is first found and given more researches on the protein structure, catalytic mechanism and practical applications, and even modified by gene engineering and protein engineering to improve its catalytic performance. In addition, also there are numerous peroxidases that are derived from various sources or used for catalytic oxidation of different substrates, which have many differences from horseradish peroxidase in amino acid composition, active site structure, catalytic characteristics and corresponding applications. To better study and selectively employ peroxidases as biocatalysts, it is critical to comprehensively recognize various peroxidases, so as to present a reference for the in-depth and accurate studies on them in the future. In this paper, various peroxidases usually focused by enzymologists are reviewed for better mastering the completed research work on them, understanding the main interests in them, and knowing the advantages and disadvantages of them. Moreover, the research aspects that hereafter may be focused on are prospected.
VL  - 5
IS  - 1
ER  -

Copy | Download