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

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 H2O2 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.

Immobilization of horseradish peroxidase on ZnO nanowires/macroporous SiO2 composites for the complete decolorization of anthraquinone dyes

“…The optimum pH for decoloring AV 109 and RB 19 was 4.5 and 5.0, respectively; the difference on the optimum pH might result from the structural feature of anthraquinone dyes; RB 19 with two SO 3 – groups was more sensitive to solution pH than AV 109 bearing one SO 3 – group. It has been reported that the free HRP showed the highest decolorization of AV 109 at pH 4.0 ; this pH shift toward alkaline zone could be ascribed to the interactions between the dyes and the support. Some reports have evidenced that support with charged surface such as Cu(II) ion incorporated membranes may alter the effect of pH on catalytic profile of enzymes .…”

“…The positively‐charged ZnO nanowires exhibited attracting force toward anthraquinone dye molecules and promoted the decolorization reaction. If the decolorization of AV 109 was catalyzed by free HRP, there would be a serious inhibitory activity from solution pH; as the pH was outside the range of 3.0–7.0, almost no decolorization efficiency could be observed . Obviously, the immobilized HRP on the nanocomposite support exhibited good activity in a more wide range of pH than did the free one, which is very important for the application.…”

“…These dyes can be hardly degraded in the environment because of their resistance to the oxidizing agents, light, and water . Recently, the decolorization of anthraquinone dyes using chloroperoxidase and horseradish peroxidase (HRP) as biocatalysts has attracted much attention because biodegradation is very effective and it is an important step for the complete removal of the pollutant . The mechanism of degradation has been studied by Liu et al , the degradation is always accompanied by decolorization which can be seen from the disappearance of characteristic adsorption.…”

Immobilization of peroxidase from fresh horseradish extract for anthraquinone dye decolorization

“…The residual amount of dye was followed using UV-Vis spectrophotometer (UV Shimadzu 1700, Shimadzu Corporation, Kyoto, Japan) at maximum wavelength for tested dye (λ max 590 nm AV 109). Decolorization was calculated using following mathematical expression [6]:…”

“…Use of horseradish peroxidase (E.C. 1.11.1.7) appeared to be very efficient as well as eco-friendly method for decolorization of wastewaters [4,[6][7][8]. Disadvantages of free enzyme application such as: instability, denaturation, impossibility of recovery and purification, contamination or proteolysis can be overcome by using their immobilized counterparts [9,10].…”