Improvement of catalytic efficiency of chloroperoxidase by its covalent immobilization on SBA-15 for azo dye oxidation

Guerrero, Esquivel; Aburto, Paulina; Terrés, E.; Villegas, Oscar; González, Eduardo; Zayas, Teresa; Hernández, Francisco; Torres, Eduardo

doi:10.1007/s10934-012-9608-8

Cited by 25 publications

(14 citation statements)

References 64 publications

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“…Km is the apparent dissociation constant, which can be treated as the overall dissociation constant of all enzyme-bound species. The Km values for hydrogen peroxide were similar than those reported for other aromatic substrates [29,39] (Table 1). At high substrate concentrations, kcat is the parameter that best describes the suitability of a substrate for a particular enzyme; however, if the substrate concentration is lower that the Km value, the better substrate for the enzyme the one which has the lower Km value [40]).…”

Section: Resultssupporting

confidence: 83%

“…This enzyme has the capability to transform compounds as different in chemical nature as pesticides [27], polycyclic aromatic hydrocarbons [28], azo dyes [29], and sulfur and nitrogen heterocyclic compounds [30,31]. The wide substrate variability of this enzyme makes it a good candidate for studies of the transformation of pharmaceutical micropollutants.…”

Section: Introductionmentioning

confidence: 99%

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Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

et al. 2018

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Abstract:The oxidation of eight pharmaceutical micropollutants by chloroperoxidase derived from Caldaromyces fumago using hydrogen peroxide as an electron acceptor is reported. All the tested compounds, namely trazadone, sulfamethoxazole, naproxen, tetracycline, estradiol, ketoconazole, ketorolac, and diclofenac, were found to be substrates for oxidation by chloroperoxidase. The respective oxidation products were identified by electrospray ionization-mass spectrometry. All the products contain at least one chloride atom in their structure after the enzymatic oxidation. Degradability experiments indicated that most of the reaction products are more biodegradable than the corresponding unmodified compounds. The enzyme was found to be catalytically active in effluent from a water treatment facility, transforming the micropollutants with high reaction rates and conversions. The enzyme was immobilized in chitosan macrospheres, which allowed the catalyst to be recycled for up to three treatment cycles in simulated samples of treated residual water. The conversion was high in the first two cycles; however, in the third, a 50% reduction in the capacity of the enzyme to oxidize ketorolac was observed. Additionally, immobilization improved the performance of the enzyme over a wider pH range, achieving the conversion of ketorolac at pH 5, while the free enzyme was not active at this pH. Overall, the results of this study suggest that chloroperoxidase represents a powerful potential catalyst in terms of its catalytic activity for the transformation of pharmaceutical micropollutants.

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Section: Resultssupporting

confidence: 83%

Section: Introductionmentioning

confidence: 99%

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

et al. 2018

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“…It has been suggested that these enzymatic treatments could oxidize the dye structures to form compounds with lower molecular weight and lower toxicity . CPO from the fungus Caldariomyces fumago was found to be very efficient for enzymatic oxidative decolorization of azo, anthraquinone and triphenylmethane‐type dye . HRP is known to degrade a wide spectrum of aromatic compounds such as phenols, anilines as well as azo dyes in the presence of H 2 O 2 .…”

Section: Introductionmentioning

confidence: 99%

A robust and stable nano‐biocatalyst by co‐immobilization of chloroperoxidase and horseradish peroxidase for the decolorization of azo dyes

Jin

Long

et al. 2017

J of Chemical Tech & Biotech

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BACKGROUND Immobilization of more than one peroxidase on the same support is an ideal technology for application because such a multi‐enzyme catalytic system may show high activity over a very wide optimal range of pH, temperature and H2O2 concentration. In this work, chloroperoxidase (CPO) and horseradish peroxidase (HRP) were co‐immobilized on ZnO nanowires/macroporous SiO2 composite support through an in situ cross‐linking method. An anionic bi‐epoxy cross‐linker was used by adsorption on the surface of ZnO nanowires before cross‐linking. RESULTS The cross‐linking was carried out under suitable conditions: pH 6.5, reaction temperature 15°C and reaction time 15 h. Using a 1/1 mixture of CPO and HRP resulted in a co‐immobilized enzyme with loading 79.6 mgCPO g‐1support and 52.8 mgHRP g‐1support, and total specific activity up to 15.7 U per mgsupport. The co‐immobilized enzyme also showed good stability after 60 days of storage, and excellent reusability over 20 repeat uses. CONCLUSIONS For the decolorization of azo dyes the co‐immobilized CPO (60%)/HRP (40%) exhibited high catalytic activity over very wide ranges of pH, temperature and H2O2 concentration. Using this robust biocatalyst, complete decolorizations of azo dyes have been realized within 3 h of reaction. © 2017 Society of Chemical Industry

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“…However, the use of CPO in large-scale industrial applications is often handicapped by a lack of long-term operational stability, difficult recovery and the inability to be recycled [5]. These drawbacks can usually be overcome by immobilization of the enzyme [6]. Furthermore, the stability, under both storage and operational conditions, e.g., towards denaturation by heat or organic solvents, can be enhanced [7].…”

Section: Introductionmentioning

confidence: 99%

“…Furthermore, the stability, under both storage and operational conditions, e.g., towards denaturation by heat or organic solvents, can be enhanced [7]. Currently, a range of supports have been reported for the immobilization of CPO, such as mesoporous supports [6,8,9], solgels [10,11], multi-walled carbon nanotubes [12,13] and other inorganic or organic solid supports [14,15]. The binding of an enzyme to a support (carrier) can be physical, ionic, or covalent in nature.…”

Section: Introductionmentioning

confidence: 99%

Bienzymatic nanoreactors composed of chloroperoxidase–glucose oxidase on Au@Fe3O4 nanoparticles: Dependence of catalytic performance on the bioarchitecture

Gao

Jiang

et al. 2016

Materials & Design

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Improvement of catalytic efficiency of chloroperoxidase by its covalent immobilization on SBA-15 for azo dye oxidation

Cited by 25 publications

References 64 publications

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

Chloroperoxidase-Mediated Halogenation of Selected Pharmaceutical Micropollutants

A robust and stable nano‐biocatalyst by co‐immobilization of chloroperoxidase and horseradish peroxidase for the decolorization of azo dyes

Bienzymatic nanoreactors composed of chloroperoxidase–glucose oxidase on Au@Fe3O4 nanoparticles: Dependence of catalytic performance on the bioarchitecture

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