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Cited by 55

The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.

Decolorization of Anthraquinonic Dyes from Textile Effluent Using Horseradish Peroxidase: Optimization and Kinetic Study

Šekuljica, Nataša Ž., Prlainović, Nevena Ž., Stefanović, Andrea B., Žuža, Milena G., Čičkarić, Dragana Z., Mijin, Dušan Ž., Knežević-Jugović, Zorica D.·2015·The Scientific World Journal
DOI 10.1155/2015/371625PMC PMC4313523
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Abstract

Two anthraquinonic dyes, C.I. Acid Blue 225 and C.I. Acid Violet 109, were used as models to explore the feasibility of using the horseradish peroxidase enzyme (HRP) in the practical decolorization of anthraquinonic dyes in wastewater. The influence of process parameters such as enzyme concentration, hydrogen peroxide concentration, temperature, dye concentration, and pH was examined. The pH and temperature activity profiles were similar for decolorization of both dyes. Under the optimal conditions, 94.7% of C.I. Acid Violet 109 from aqueous solution was decolorized (treatment time 15 min, enzyme concentration 0.15 IU/mL, hydrogen peroxide concentration 0.4 mM, dye concentration 30 mg/L, pH 4, and temperature 24°C) and 89.36% of C.I. Acid Blue 225 (32 min, enzyme concentration 0.15 IU/mL, hydrogen peroxide concentration 0.04 mM, dye concentration 30 mg/L, pH 5, and temperature 24°C). The mechanism of both reactions has been proven to follow the two substrate ping‐pong mechanism with substrate inhibition, revealing the formation of a nonproductive or dead‐end complex between dye and HRP or between H 2 O 2 and the oxidized form of the enzyme. Both chemical oxygen demand and total organic carbon values showed that there was a reduction in toxicity after the enzymatic treatment. This study verifies the viability of use of horseradish peroxidase for the wastewaters treatment of similar anthraquinonic dyes.

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Figures

Figure 1 Time course of decolorization of AV 109 (circle) and AB 225 (square) dyes at concentration of 30 mg/L. Other reaction conditions for AV 109 dye: peroxide concentration 2 mM, pH 5.25, enzyme concentration 0.15 IU/mL, temperature 24°C; for AB 225 dye: hydrogen peroxide concentration 1 mM, pH 5.5, enzyme concentration 0.04 IU/mL, and temperature 24°C.
Figure 1 Time course of decolorization of AV 109 (circle) and AB 225 (square) dyes at concentration of 30 mg/L. Other reaction conditions for AV 109 dye: peroxide concentration 2 mM, pH 5.25, enzyme concentration 0.15 IU/mL, temperature 24°C; for AB 225 dye: hydrogen peroxide concentration 1 mM, pH 5.5, enzyme concentration 0.04 IU/mL, and temperature 24°C.CC BY · PubMed Central
Figure 2 Absorption spectra before (solid lines) and after enzymatic decolorization experiment (dotted lines) for AB 225 (blue) and AV 109 (violet).
Figure 2 Absorption spectra before (solid lines) and after enzymatic decolorization experiment (dotted lines) for AB 225 (blue) and AV 109 (violet).CC BY · PubMed Central
Figure 3 (a) Time course of decolorization of AB 225 and (b) AV 109 dyes at different initial enzyme concentration. (c) The influence of the initial enzyme concentration on the decolorization percentage for AB 225 and (d) AV 109. Reaction conditions for AB 225: treatment time 32 minutes, dye concentration 30 mg/L, hydrogen peroxide concentration 1 mM, pH 5.25, temperature 24°C, and for AV 109: treatment time 15 minutes, dye concentration 30 mg/L, hydrogen peroxide concentration 2 mM, temperature 24°C, pH 5.5. Each value represents the average of three experiments.
Figure 3 (a) Time course of decolorization of AB 225 and (b) AV 109 dyes at different initial enzyme concentration. (c) The influence of the initial enzyme concentration on the decolorization percentage for AB 225 and (d) AV 109. Reaction conditions for AB 225: treatment time 32 minutes, dye concentration 30 mg/L, hydrogen peroxide concentration 1 mM, pH 5.25, temperature 24°C, and for AV 109: treatment time 15 minutes, dye concentration 30 mg/L, hydrogen peroxide concentration 2 mM, temperature 24°C, pH 5.5. Each value represents the average of three experiments.CC BY · PubMed Central
Figure 4 The decolorization percentage as a function of H2O2 concentration (a) and dye concentration (b). Reaction conditions for AB 225: reaction time 32 minutes, enzyme concentration 0.15 IU/mL, pH 5.25, and temperature 24°C; for AV 109: reaction time 15 minutes, enzyme concentration 0.15 IU/mL, pH 5.5, and temperature 24°C.
Figure 4 The decolorization percentage as a function of H2O2 concentration (a) and dye concentration (b). Reaction conditions for AB 225: reaction time 32 minutes, enzyme concentration 0.15 IU/mL, pH 5.25, and temperature 24°C; for AV 109: reaction time 15 minutes, enzyme concentration 0.15 IU/mL, pH 5.5, and temperature 24°C.CC BY · PubMed Central
Figure 5 The influence of the initial pH on AB 225 and AV 109 decolorization at 24°C with 0.15 IU/mL HRP. Reaction conditions for AB 225: 32 minutes, dye concentration 30 mg/L, and hydrogen peroxide concentration 0.04 mM; for AV 109: 15 minutes, dye concentration 30 mg/L, and hydrogen peroxide concentration 0.4 mM. Relative standard deviations (RSD) of triplicate measurements were always less than 5%.
Figure 5 The influence of the initial pH on AB 225 and AV 109 decolorization at 24°C with 0.15 IU/mL HRP. Reaction conditions for AB 225: 32 minutes, dye concentration 30 mg/L, and hydrogen peroxide concentration 0.04 mM; for AV 109: 15 minutes, dye concentration 30 mg/L, and hydrogen peroxide concentration 0.4 mM. Relative standard deviations (RSD) of triplicate measurements were always less than 5%.CC BY · PubMed Central
Figure 6 The influence of temperature on AB 225 and AV 109 decolorization. Other reaction conditions were optimal for both dyes.
Figure 6 The influence of temperature on AB 225 and AV 109 decolorization. Other reaction conditions were optimal for both dyes.CC BY · PubMed Central
Figure 7 (a) Initial rate versus hydrogen peroxide concentration at fixed AV 109 concentration of 0.018 mM and (b) initial rate versus AV 109 concentration at fixed hydrogen peroxide concentration of 0.06 mM. Symbols represent experimental data, lines indicate kinetic models based on fitted kinetic parameters including substrate inhibition (solid lines) and without substrate inhibition (dotted lines).
Figure 7 (a) Initial rate versus hydrogen peroxide concentration at fixed AV 109 concentration of 0.018 mM and (b) initial rate versus AV 109 concentration at fixed hydrogen peroxide concentration of 0.06 mM. Symbols represent experimental data, lines indicate kinetic models based on fitted kinetic parameters including substrate inhibition (solid lines) and without substrate inhibition (dotted lines).CC BY · PubMed Central
Figure 8 (a) Initial rate versus hydrogen peroxide concentration at fixed AB 225 concentration of 0.029 mM and (b) initial rate versus AB 225 concentration at fixed hydrogen peroxide concentration of 0.1 mM. Symbols represent experimental data, lines indicate kinetic models based on fitted kinetic parameters including substrate inhibition (solid lines) and without substrate inhibition (dotted lines).
Figure 8 (a) Initial rate versus hydrogen peroxide concentration at fixed AB 225 concentration of 0.029 mM and (b) initial rate versus AB 225 concentration at fixed hydrogen peroxide concentration of 0.1 mM. Symbols represent experimental data, lines indicate kinetic models based on fitted kinetic parameters including substrate inhibition (solid lines) and without substrate inhibition (dotted lines).CC BY · PubMed Central
Scheme 1 Schematic representation of the ping-pong bi-bi mechanism with dye and H2O2 inhibition.
Scheme 1 Schematic representation of the ping-pong bi-bi mechanism with dye and H2O2 inhibition.CC BY · PubMed Central

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Citations

Cites

Research works printed but not linked: 2

  1. Gholami-Borujeni F., 2013, Oxidative degradation and detoxification of textile azo dye by horseradish peroxidase enzyme, Fresenius Environmental Bulletin, 22, 739
  2. 10.1002/1097-0290(20010305)72:5x003C;562::aid-bit1020x0003e;3.3.co;2-j · DOI

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Metadata

Authors
Šekuljica, N. Ž., Prlainović, N. Ž., Stefanović, A. B., Žuža, M. G., Čičkarić, D. Z., Mijin, D. Ž., & Knežević-Jugović, Z. D.
Venue
The Scientific World Journal
Publisher
Wiley
Published
2015-01
Volume
2015
Issue
1
ISSN
  • 2356-6140
  • 1537-744X
DOI
10.1155/2015/371625
PMC
PMC4313523
Cited by
55
References
38
Language
en
Licence
creativecommons.org/licenses/by/3.0/ (vor, 18 d)
Funders
Ministry of Education, Science and Technological Development (III-46010 and 172013)

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