Izvestiya of Saratov University.

Chemistry. Biology. Ecology

ISSN 1816-9775 (Print)
ISSN 2541-8971 (Online)


For citation:

Solovyeva A. A., Lebedeva O. E., Thi Pham T. Evaluation of activity of peroxidases contained in various plant sources. Izvestiya of Saratov University. Chemistry. Biology. Ecology, 2023, vol. 23, iss. 4, pp. 472-478. DOI: 10.18500/1816-9775-2023-23-4-472-478, EDN: SSYFHT

This is an open access article distributed under the terms of Creative Commons Attribution 4.0 International License (CC-BY 4.0).
Full text:
(downloads: 77)
Language: 
Russian
Heading: 
Article type: 
Article
UDC: 
544.47:542.943:615.322
EDN: 
SSYFHT

Evaluation of activity of peroxidases contained in various plant sources

Autors: 
Solovyeva Anna A., Federal State Autonomous Educational Institution of Higher Education
Lebedeva Olga E., Federal State Autonomous Educational Institution of Higher Education
Thi Pham Trinh, Federal State Autonomous Educational Institution of Higher Education
Abstract: 

In this study, the decolorization reaction of aqueous solution bromophenol blue dye was carried out in the presence of hydrogen peroxide and peroxidase contained in the roots of horseradish (Armoracia rusticana), radish (Raphanus sativus var. radicula), yellow turnip (Brassica napobrassica), daikon (Raphanus sativus), black radish (Raphanus sativus ‘Niger’), green radish (Raphanus) or stalk of white cabbage (Brassica capitata). The reaction was carried out at an initial dye content of 25,1 μM, a hydrogen peroxide concentration of 0,4 mM, at t = 24 °C and pH 4,01, the peel of various vegetables was used as a source of peroxidase; it was inserted into the reaction without enzyme primary extraction. When using horseradish waste, black radish, white cabbage, turnips, it is possible to get the degree of decolorization of the dye in its aqueous solution by 95%. The maximum rate and Michaelis constants of the enzymatic reaction are calculated by the linearization method in the Linuiver – Burke coordinates. It is shown that the activity of peroxidase contained in the peel of black radish persists with an increase in temperature from 23 to 40 °С.

Reference: 
  1. Selvaraj V., Karthika T. S., Mansiya C., Alagar M. An over a review of recently developed techniques, mechanisms, and intermediate involved in the advanced azo dye degradation for industrial applications // J. Mol. Struct. 2021. Vol. 1224. P. 129–195. https://doi.org/10.1016/j.molstruc.2020.129195
  2. Routoula E., Patwardhan S. V. Degradation of anthraquinone dyes from effl uents: A review focusing on enzymatic dye degradation with industrial potential // Environ. Sci. Technol. 2019. Vol. 54, № 2. P. 647–664. https://doi.org/10.1021/acs.est.9b03737
  3. Singh R. L., Singh P. K., Singh R. P. Enzymatic decolorization and degradation of azo dyes. A review // Int. Biodeterior. Biodegradation. 2015. Vol. 104. P. 21–31. https://doi.org/10.1016/j.ibiod.2015.04.027
  4. Imran M., Crowley D. E., Khalid A. Microbial biotechnology for decolorization of textile wastewaters // Environ. Sci. Biotechnol. 2015. Vol. 14. P. 73–92. https://doi.org/10.1007/s11157-014-9344-4
  5. Baumer J. D., Valerio A., Guelli Ulson de Souza S. M., Erzinger G. S., Furigo Jr A., Ulsonde Souza A. A. Toxicity of enzymatically decolored textile dyes solution by horseradish peroxidase // J. Hazard. Mater. 2018. Vol. 360. P. 82–88. https://doi.org/10.1016/j.jhazmat.2018.07.102
  6. Sekuljica N. Z., Prlainovic N. Z., Jakovetic S. M., Grbavcic S. Z., Ognjanovic N. D., Knezevic-Jugovic Z. D., Mijin D. Z. Removal of anthraquinone dye by cross-linked enzyme aggregates from fresh horseradish extract // Clean: Soil, Air, Water. 2016. Vol. 44. Р. 1–10. https://doi.org/10.1002/clen.201500766
  7. Terres J., Battisti R., Andreaus J., Cesar de Jesus P. Decolorization and degradation of Indigo Carmine dye from aqueous solution catalyzed by horseradish peroxidase // Biocatal. Biotransform. 2014. Vol. 32, № 1. P. 64–73. https://doi.org/10.3109/10242422.2013.873416 
  8. Farias S., de Oliveira D., Ulson de Souza A. A., Guelli U. de Souza S. M., Morgado F. Removal of reactive blue 21 and reactive red 195 dyes using horseradish peroxidase as catalyst // Brazil. J. Chem. Eng. 2017. Vol. 34, № 3. P. 701–707. https://doi.org/10.1590/0104- 6632.20170343s20160091
  9. Вяткина О. В. Проблемы выделения и очистки растительных пероксидаз // Ученые записки Крымского федерального университета им. В. И. Вернадского. Биология. Химия. 2012. Т. 25 (64), № 3. С. 271–276.
  10. Ahmedi A., Abouseoud M., Couvert A., Amrane A. Enzymatic degradation of Congo Red by turnip (Brassica rapa) peroxidase // Zeitschrift für Naturforschung. 2012. Vol. 67, № 7-8. P. 429 –436. https://doi.org/10.5560/ ZNC.2012.67c0429
  11. Bania I., Mahanta R. Evaluation of peroxidases from various plant sources // International Journal of Scientifi c and Research Publications. 2012. Vol. 2, iss. 5. P. 1–5.
  12. Poloznikov A. A., Zakharova G. S., Chubar T. A., Tishkov V. I., Gazaryan I. G. Site-directed mutagenesis of tobacco anionic peroxidase: Effect of additional aromatic acids on stablity and activity // Biochimie. 2015. Vol. 115, № 1. P. 71–77. https://doi.org/10.1016/j. biochi.2015.04.021
  13. Gaspar S., Popescu I. C., Gazaryan I. G., Csöregi E. Biosensors based on novel plant peroxidases: A comparative study // Electrochimica Acta. 2000. Vol. 46, № 2-3. P. 255–264. https://doi.org/10.1016/S0013- 4686(00)00580-6
  14. Thongsook T., Barrett D. Purification and partial characterization of broccoli (Brassica oleracea var. Italica) peroxidases // Journal of Agricultural and Food Chemistry. 2005. Vol. 53, № 8. P. 3206–3214. https://doi. org/10.1021/jf048162s
  15. Somtürk B., Kalın R., Özdemir N. Purification of Peroxidase from Red Cabbage (Brassica oleracea var. capitata f. rubra) by Affi nity Chromatography // Applied Biochemistry and Biotechnology. 2014. Vol. 173, № 7. P. 1815–1828. https://doi.org/10.1007/s12010-014-0968-1
  16. Riaz A., Kalsoom U., Bhatti H. N., Jesionowski T., Bilal M. Citrus limon peroxidase-assisted biocatalytic approach for biodegradation of reactive 1847 colfax blue P3R and 621 colfax blue R dyes // Bioprocess and Biosystems Engineering. 2023. Vol. 46. P. 443–452. https://doi. org/10.1007/s00449-022-02802-z
  17. Соловьева А. А., Фам Т. Ч., Лебедева О. Е., Устинова М. Н. Деструкция бромфенолового синего с участием пероксидазы хрена // Известия высших учебных заведений. Серия: Химия и химическая технология. 2021. Т. 64, № 1. С. 93–98. https://doi.org/10.6060/ivkkt.20216401.6267
  18. Никитенко А. Н., Егорова З. Е. Изменение активности полифенолоксидазы, аскорбиноксидазыи пероксидазы в процессе хранения яблок // Труды БГТУ. Химия, технология органических веществ и биотехнология. 2011. № 4. С. 216–219.
  19. Щербаков В. Г., Лобанов В. Г., Прудникова Т. Н. Биохимия / под ред. В. Г. Щербакова. 2-е изд. СПб. : ГИОРД, 2003. 440 с.
  20. Степуро М. В., Квитайло И. В., Шутова К. С. Влияние температуры и рН среды на активность пероксидазы, выделенной из топинамбура // Известия вузов. Пищевая технология. 2010. № 1. С. 120–121. 
Received: 
12.05.2023
Accepted: 
07.08.2023
Published: 
25.12.2023
Short text (in English):
(downloads: 52)