Skip to main content
SpringerLink
Log in

Modeling and simulation of the enzymatic degradation of 2,4,6-trichlorophenol using soybean peroxidase

  • Original Paper
  • Published:
Brazilian Journal of Chemical Engineering Aims and scope Submit manuscript

Abstract

The enzymatic degradation of organic pollutants is a promising and ecological method for the remediation of industrial effluents. 2,4,6-Trichlorophenol is a major pollutant in many residual waters, and its consumption has been linked to lymphomas, leukemia, and liver cancer. The goal of the present work is to comprehend the enzymatic degradation of 2,4,6-trichlorophenol using soybean peroxidase. Different assumptions for the kinetic model were evaluated, and the simulations were compared to experimental data, which was obtained in a microreactor. The literature pointed out that the bi-bi ping-pong model represents well the kinetics of soybean peroxidase degradation. Since it is a complex model, some reactions can be considered or not. Six different possibilities for the model were considered, regarding different combinations of the generated enzyme forms that depend on the hypotheses for simplifying the model. The adjustment of the models was compared based on different metrics, such as the value of the objective function, coefficient of determination and root-mean-square error. The process modeling was obtained by the mass balance of all the reaction components, and all the simulations were performed in MATLAB R2015a. Reaction parameters were estimated based on the weighted least squares between the experimental data set and the values predicted by the model. The results showed that the data were better adjusted by the model that considers all the enzyme forms, including enzyme inactivation. Therefore, a better comprehension of the reaction mechanism was achieved, which allows a more precise reactor project and process simulation.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7
Fig. 8

Similar content being viewed by others

References

  • Adediran A, Lambeir A (1989) Kinetics of the reaction of compound I1 of horseradish peroxidase with hydrogen peroxide to form compound III. Eur J Biochem 186:571–576

    Article  CAS  Google Scholar 

  • Al-Ansari MM, Saha B, Mazloum S, Taylor KE, Bewtra JK, Biswas N (2011) Soybean peroxidase applications in wastewater treatment. In: Maxwell JE (ed) Soybeans: Cultivation, Uses and Nutrition, Nova Science Publishers, Inc., Hauppauge, NY, pp 189–221

  • Arnao MB, Acosta M, del Rio JA, Varon R, Garcia-Canovas F (1990) A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide. Biochim Biophys Acta 1041:43–47

    Article  CAS  Google Scholar 

  • Bassi A, Geng Z, Gijzen M (2004) Enzymatic Removal of Phenol and Chlorophenols Using Soybean Seed Hulls. Eng Life Sci 4:125–130

    Article  CAS  Google Scholar 

  • Buchanan ID, Nicell JA (1997) Model Development for Horseradish Peroxidase Catalyzed Removal of Aqueous Phenol. Biotechnol Bioeng 54(3):251–261

  • Calza P, Avetta P, Rubulotta G, Sangermano M, Laurenti E (2014) TiO2-soybean peroxidase composite materials as a new photocatalytic system. Chem Eng J 239:87–92

    Article  CAS  Google Scholar 

  • Calza P, Zacchigna D, Laurenti E (2016) Degradation of orange dyes and carbamazepine by soybean peroxidase immobilized on silica monoliths and titanium dioxide. Environ Sci Pollut Res 23(23):23742–23749

    Article  CAS  Google Scholar 

  • Costa RA, Cunha AS, Peres JCG, Azzoni AR, Laurenti E, Vianna AS (2020) Enzymatic Degradation of 2,4,6-Trichlorophenol in a Microreactor using Soybean Peroxidase. Symmetry 12:1129

    Article  CAS  Google Scholar 

  • Ferrari RP, Laurenti E, Trotta F (1999) Oxidative 4-dechlorination of 2,4,6-trichlorophenol catalyzed by horseradish peroxidase. J Biol Inorg Chem 4(2):232–237

    Article  CAS  Google Scholar 

  • Fersht A (1999) Structure and mechanism in protein science: A guide to enzyme catalysis and protein folding, vol 13409. W.H.Freeman and Co Ltd, New York

  • Gacche RN, Firdaus Q, Sagar AD (2003) Soybean (Glycine max L.) seed coat peroxidase immobilized on fibrous aromatic polyamide: a strat-egy for decreasing phenols from industrial wastewater. J Sci Ind Res (India) 62:1090–1093

    CAS  Google Scholar 

  • Ghaemmaghami F, Alemzadeh I, Motamed S (2010) Seed coat Soybean peroxidase: extraction and biocatalytic properties determination. Iran J Chem Eng 7(2):28–38

    Google Scholar 

  • Gowdal TPH, Lock JD, Kurtz RG (1985) A comprehensive study of risk assessment for a hazardous compound of public health concern. Water Air Soil Pollut 24:189–206

  • Graham JS, Xiong J, Gillikin JW (1991) Purification and developmental analysis of a metalloendoproteinase from the leaves of Glycine max. Plant Physiol 97(2):786–792

    Article  CAS  Google Scholar 

  • Husain Q (2010) Peroxidase mediated decolorization and remediation of wastewater containing industrial dyes: a review. Rev Environ Sci Biotechnol 9:117–140

    Article  CAS  Google Scholar 

  • Job D, Dunford HB (1976) Substituent effect on the oxidation of phenols and aromatic amines by horseradish peroxidase compound I. Eur J Biochem 66:607–614

    Article  CAS  Google Scholar 

  • Laurenti E, Vianna AS Jr (2016) Enzymatic microreactors in biocatalysis: history, features, and future perspectives. Biocatalysis 1(1):148–165

  • Laurenti E, Ghibaudi E, Todaro G, Ferrari RP (2002) Enzymatic degradation of 2,6-dichlorophenol by horseradish peroxidase. J Inorg Biochem 92:75–81

    Article  CAS  Google Scholar 

  • Laurenti E, Ghibaudi E, Ardissone S, Ferrari RP (2003) Oxidation of 2,4-dichlorophenol catalyzed by horseradish peroxidase: Characterization of the reaction mechanism by UV-visible spectroscopy and mass spectrometry. J Inorg Biochem 95(2–3):171–176

  • Nakajima R, Yamazaki I (1987) The mechanism of oxyperoxidase formation from ferry1 peroxidase and hydrogen peroxide. J Biol Chem 262:2576–2581

    Article  CAS  Google Scholar 

  • Nicell JA (1994) Kinetics of horseradish peroxidase‐catalysed polymerization and precipitation of aqueous 4‐chlorophenol. J Chem Technol Biotechnol 60(2):203–215

    Article  CAS  Google Scholar 

  • Nicell J, Wright H (1997) A model of peroxidase activity with inhibition by hydrogen peroxide. Enzyme Microb Technol 21:302–310

    Article  CAS  Google Scholar 

  • Nissum M, Schiodt CB, Welinder KG (2001) Reactions of soybean peroxidase and hydrogen peroxide pH 2.4-12.0, and veratryl alcohol at pH 2.4. Biochimica et Biophysica Acta Prot Struct Mol Enzymol 1545(1–2):339–348

    Article  CAS  Google Scholar 

  • Sakurada J, Sekiguchi R, Sato K, Hosoya T (1990) Kinetic and molecular orbital studies on the rate of oxidation of monosubstituted phenols and anilines by horseradish peroxidase compound II. Biochemistry 29:4093–4098

    Article  CAS  Google Scholar 

  • Sharma B, Dangi AK, Shukla P (2018) Contemporary enzyme based technologies for bioremediation: A review. J Environ Manag 210:10–22

    Article  CAS  Google Scholar 

  • Silva MC, Torres JA, Vasconcelos de Sá LR, Chagas PMB, Ferreira-Leitão VS, Corrêa AD (2013) The use of soybean peroxidase in the decolourization of Remazol Brilliant Blue R and toxicological evaluation of its degradation products. J Mol Catal B Enzym 89:122–129

    Article  CAS  Google Scholar 

  • Steevensz A, Madur S, Al-Ansari MM, Taylor KE, Bewtra JK, Biswas N (2013) A simple lab-scale extraction of soybean hull peroxidase shows wide variation among cultivars. Ind Crops Prod 48:13–18

    Article  CAS  Google Scholar 

  • Steevensz A, Cordova Villegas LG, Feng W, Taylor KE, Bewtra JK, Biswas N (2014) Soybean peroxidase for industrial wastewater treatment: a mini review. J Environ Eng Sci 9(3):181–186

    Article  Google Scholar 

  • Tamura Y, Yamazaki I (1972) Reactions of the oxyform of horseradish peroxidase. J Biochem 71:311–319

    Article  CAS  Google Scholar 

  • Tchobanoglous G, Burton FL, Stensel HD (2014) Wastewater engineering: treatment and resource recovery, 5th edn. McGraw-Hill, New York

  • Tolardo V, García-Ballesteros S, Santos-Juanes L, Vercher R, Amat AM, Arques A, Laurenti E (2019) Pentachlorophenol Removal from Water by Soybean Peroxidase and Iron(II) Salts Concerted Action. Water Air Soil Pollut 230:140

  • Torres E, Ayala M (2010) Biocatalysis based on heme peroxidases. Peroxidases as potential industrial biocatalysts, 1st edn. Springer, Berlin

  • Yamazaki I, Nakajima R (1986) Physico-chemical comparison between horseradish peroxidases A and C. In: Greppin H, Penel C, Gaspar T (eds) Molecular and Physiological Aspects of Plant Peroxidases, 3rd edn, University of Geneva, Switzerland, pp 71–84

  • Zhang Y, Liu M, Liu J, Wang X, Wang C, Ai W, Chen S, Wang H (2018) Combined toxicity of triclosan, 2,4-dichlorophenol and 2,4,6-trichlorophenol to zebrafish (Danio rerio). Environ Toxicol Pharmacol 57:9–18

    Article  CAS  Google Scholar 

Download references

Acknowledgements

The author thanks CAPES Finance Code 001 for financial support.

Author information

Authors and Affiliations

  1. Department of Chemical Engineering, University of São Paulo, 05508010, São Paulo, Brazil

    Alexandre Santuchi da Cunha & Ardson dos S. Vianna Jr.

  2. Department of Chemistry, Università di Torino, 10125, Turin, Italy

    Enzo Laurenti

Authors
  1. Alexandre Santuchi da Cunha
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ardson dos S. Vianna Jr.
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Enzo Laurenti
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Alexandre Santuchi da Cunha.

Ethics declarations

Conflict of interest

The authors declare they have no conflict of interest.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

da Cunha, A.S., dos S. Vianna Jr. , A. & Laurenti, E. Modeling and simulation of the enzymatic degradation of 2,4,6-trichlorophenol using soybean peroxidase. Braz. J. Chem. Eng. 38, 719–730 (2021). https://doi.org/10.1007/s43153-021-00135-0

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s43153-021-00135-0

Keywords

Search

Navigation