A Mass Spectrometric Investigation of Native and Oxidatively Inactivated Chloroperoxidase

Grey, Carl; Hedström, Martin; Adlercreutz, Patrick

doi:10.1002/cbic.200700091

Cited by 36 publications

(17 citation statements)

References 75 publications

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“…Low concentration of H 2 O 2 cannot supply sufficient oxidant for enzymatic oxidative degradation of the drug. However, high concentration of H 2 O 2 is also not favorable for CPO due to the inactivation caused by internal oxidative destruction of the porphyrin moiety . According to the results in Fig.…”

Section: Resultsmentioning

confidence: 87%

Combination of enzymatic degradation by chloroperoxidase with activated sludge treatment to remove sulfamethoxazole: performance, and eco-toxicity assessment

Xiao

Jiang

et al. 2016

J. Chem. Technol. Biotechnol.

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BACKGROUND Sulfamethoxazole is found in surface and ground waters because it is usually not metabolized and simply passes through the human body after ingestion. This drug is difficult to degrade by conventional treatments and may cause environmental concerns. RESULTS A rapid and efficient enzymatic degradation of sulfamethoxazole by a heme peroxidase, chloroperoxidase (CPO), was investigated in this work. The degradation efficiency of sulfamethoxazole reached 98.64% within 20 min at room temperature, atmospheric pressure and environment‐friendly reaction conditions with an enzyme concentration of approximately 10−9 mol L−1. High performance liquid chromatography–mass spectrometry analysis was employed to identify the intermediates and final products. Moreover, chemical oxygen demand (COD) measurements showed that pre‐treatment by CPO‐H2O2 oxidative degradation followed by existing bioremediation technologies can effectively improve the efficiency and thoroughness of decontaminating this drug from wastewater. The degradation efficiency was enhanced from 76.5% to 84.47%, and the COD removal increased from 29.72% to 51.32%. The eco‐toxicity test using a green algae, Chlorella pyrenoidos, showed that the degraded products had lower toxicity than the parent drug. CONCLUSION CPO catalyzed oxidative degradation is a promising alternative for treatment of wastewater containing sulfonamide drugs. This enzymatic method is also suitable for treatment of other sulfonamide antibiotics. © 2016 Society of Chemical Industry

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Section: Resultsmentioning

confidence: 87%

Combination of enzymatic degradation by chloroperoxidase with activated sludge treatment to remove sulfamethoxazole: performance, and eco-toxicity assessment

Xiao

Jiang

et al. 2016

J. Chem. Technol. Biotechnol.

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“…In fact, hydrogen peroxide is a compound capable of afecting the enzyme chemical structure, mainly at high concentrations [56]. It is able to modify many of the aminoacids of a protein (Arg, Pro, Lys, Met, Cys, Tyr, His, etc), even cleaving the peptidic bonds in some cases [57].…”

mentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

140

107

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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“…It is well known now that a high concentration of H 2 O 2 is not favorable for enzymatic reaction catalyzed by heme proteins, such as cytochrome P450, horseradish peroxidase and CPO . This was due to the irreversible inactivation which was mainly caused by internal oxidative destruction of the porphyrin moiety .…”

Section: Resultsmentioning

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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A Mass Spectrometric Investigation of Native and Oxidatively Inactivated Chloroperoxidase

Cited by 36 publications

References 75 publications

Combination of enzymatic degradation by chloroperoxidase with activated sludge treatment to remove sulfamethoxazole: performance, and eco-toxicity assessment

Combination of enzymatic degradation by chloroperoxidase with activated sludge treatment to remove sulfamethoxazole: performance, and eco-toxicity assessment

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

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

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