Decolorization and degradation of Indigo Carmine dye from aqueous solution catalyzed by horseradish peroxidase

Terres, Josias; Battisti, Rodrigo; Andreaus, Jürgen; Jesus, Paulo César de

doi:10.3109/10242422.2013.873416

Cited by 24 publications

(17 citation statements)

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“…Similarly, SBP appears to work well at 25°C; however, a slight increase in degradation of Trypan Blue dye was observed on increasing the temperature up to 50°C [88]. Terres et al [90] reported that the aqueous solutions of Indigo Carmine dye catalyzed by the enzyme horseradish peroxidase (HRP) were decolorized at temperatures between 40 and 60°C. Maximum color removal of C.I.…”

Section: Effect Of Temperaturementioning

confidence: 95%

“…Beyond which, the degradation of dye is decreasing abruptly as the concentration of dye increases [92]. Terres et al [90] reported that a dye concentration of 2.5×10 −5 mol/l of Indigo Carmine dye was decolorized by 2 mg of horseradish peroxidase.…”

Section: Optimum Concentration Of Dyementioning

confidence: 97%

“…Ali et al [89] reported that the soybean peroxidase enzyme was most active in the pH range of 3-5 for degradation of Crystal Ponceau 6R dye. Terres et al [90] reported that the aqueous solutions of Indigo Carmine dye catalyzed by the enzyme horseradish peroxidase (HRP) were decolorized at pH 4, 5, and 6. Gholami-Borujeni et al [91] evaluated that decolorization of acid blue-25 (AB-25) dye with horseradish peroxidase was maximum at pH 7 and 0.8.…”

Section: Effect Of Phmentioning

confidence: 99%

“…Acid Blue 113 dye was maximally degraded with 0.08 U of horseradish peroxidase in 45 min of contact time. An aqueous solution of 2.5×10 −5 mol/l of Indigo Carmine dye was decolorized by horseradish peroxidase (HRP) between 30 and 60 min of contact time [90]. Gholami-Borujeni et al [91] determined that 75-min contact time was optimum for horseradish peroxidase catalyzed decolorization of acid blue-25 (AB-25) dye.…”

Section: Optimum Contact Timementioning

confidence: 99%

“…Acid Blue 113 dye up to 80 % [92]. A dye concentration of 2.5×10 −5 mol/l of Indigo Carmine dye was decolorized by 2 mg of horseradish peroxidase [90].…”

Section: Optimum Dose Of Enzymementioning

confidence: 99%

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Characterization of Plant Peroxidases and Their Potential for Degradation of Dyes: a Review

Kalsoom

Bhatti

Asgher

2015

Appl Biochem Biotechnol

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Peroxidases are ubiquitously found in all vascular plants and are promising biocatalysts for oxidization of wide range of aromatic substrates including various industrial dyes. Peroxidases can catalyze degradation of chemical structure of aromatic dyes either by precipitation or by opening the aromatic ring structure. Both soluble and immobilized peroxidases have been successfully used in batches as well as in continuous processes for the treatment of aromatic dyes present in industrial effluents. Plant peroxidases are stable catalysts that retain their activities over a broad range of pH and temperatures. The performance of an enzyme for degradation process depends upon the structure of dyes and the operational parameters like concentration of enzyme, H2O2 and dye, incubation time, pH, and temperature. Recalcitrant dyes can also be mineralized by plant peroxidases in the presence of redox mediators. Thus, plant peroxidases are easily available, inexpensive, and ecofriendly biocatalysts for the treatment of wastewaters containing a wide spectrum of textile and non-textile synthetic dyes. This article reviews the recent developments in isolation and characterization of plant peroxidases and their applications for bioremediation of synthetic dyes.

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Section: Effect Of Temperaturementioning

confidence: 95%

Section: Optimum Concentration Of Dyementioning

confidence: 97%

Section: Effect Of Phmentioning

confidence: 99%

Section: Optimum Contact Timementioning

confidence: 99%

“…Acid Blue 113 dye up to 80 % [92]. A dye concentration of 2.5×10 −5 mol/l of Indigo Carmine dye was decolorized by 2 mg of horseradish peroxidase [90].…”

Section: Optimum Dose Of Enzymementioning

confidence: 99%

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