Development of a microbial bioassay for chlorinated and brominated hydrocarbons

Hutter, W.; Peter, Jyotsna Kiran; Swoboda, H.; Hampel, W.; Rosenberg, Erwin; Krämer, Dietmar; Kellner, Robert

doi:10.1016/0003-2670(94)00679-g

Cited by 23 publications

(14 citation statements)

References 12 publications

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“…LinA catalyses dehydrochlorination of halophenols, such as lindane, generating less chlorinated products that can be dechlorinated hydrolytically by LinB (Longoria et al, 2008;Szatkowski et al, 2011;Wannstedt et al, 1990). LinB has also been described as having catalytic activity against some CAHs (Campbell et al, 2006;Hutter et al, 1995;Mazurenko et al, 2018;Shahar et al, 2019aShahar et al, , 2019b. Also recognised as having high detoxification potential, heme-containing enzymes, like dehaloperoxidase (DHP) and horseradish peroxidase (HRP), catalyse oxidative dehalogenation of halophenols to their corresponding quinones (Longoria et al, 2008;Wannstedt et al, 1990), but can also be inhibited by several HOCs, revealing the complex biological interactions of such compounds (Szatkowski et al, 2011).…”

Section: Figmentioning

confidence: 99%

“…To screen the enzymatic activity, numerous analytical techniques are usually utilized downstream the biochemical reaction. As summarized in Table 4, biosensing strategies, based on chromatographic (Bidmanova et al, 2016;Brack et al, 2002;Shimizu et al, 2013), electrochemical (Anu Prathap et al, 2012Besombes et al, 1995;Kaur et al, 2016;Kim et al, 2008;McArdle and Persaud, 1993;Miao et al, 2016;Nomngongo et al, 2012;Vidal et al, 2008;Wu, 2011;Xia et al, 2015;Xu et al, 2019), potentiometric (Hutter et al, 1995), conductimetric (Anh et al, 2004), spectrophotometric (de Souza et al, 2018Hipólito-Moreno et al, 1998;Q. Liu et al, 2019;Mazurenko et al, 2018;McArdle and Persaud, 1993;Shahar et al, 2019a;Silva et al, 2015) and fluorescence spectroscopic methods (Bidmanova et al, 2016(Bidmanova et al, , 2010Campbell et al, 2006;Mazurenko et al, 2018;Sok and Fragoso, 2018) can be found in literature.…”

Section: Enzymatic Biosensors For Hocs Determinationmentioning

confidence: 99%

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Enzymatic assays for the assessment of toxic effects of halogenated organic contaminants in water and food. A review

Artabe

Cunha-Silva

Barranco

2020

Food and Chemical Toxicology

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Halogenated organic compounds are a particular group of contaminants consisting of a large number of substances, and of great concern due to their persistence in the environment, potential for bioaccumulation and toxicity. Some of these compounds have been classified as persistent organic pollutants (POPs) under The Stockholm Convention and many toxicity assessments have been conducted on them previously. In this work we provide an overview of enzymatic assays used in these studies to establish toxic effects and dose-response relationships. Studies in vivo and in vitro have been considered with a particular emphasis on the impact of halogenated compounds on the activity of relevant enzymes to the humans and the environment. Most information available in the literature focuses on chlorinated compounds, but brominated and fluorinated molecules are also the target of increasing numbers of studies. The enzymes identified can be classified as enzymes: i) the activities of which are affected by the presence of halogenated organic compounds, and ii) those involved in their metabolisation/detoxification resulting in increased activities. In both cases the halogen substituent seems to have an important role in the effects observed. Finally, the use of these enzymes in biosensing tools for monitoring of halogenated compounds is described.

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Section: Figmentioning

confidence: 99%

Section: Enzymatic Biosensors For Hocs Determinationmentioning

confidence: 99%

Enzymatic assays for the assessment of toxic effects of halogenated organic contaminants in water and food. A review

Artabe

Cunha-Silva

Barranco

2020

Food and Chemical Toxicology

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“… Biotechnological applications of HLDs. Summary of reported applications of DatA [35], DbeA (Prudnikova et al, in preparation), DbjA [45, 47, 57, 61, 63, 125], DhaA [14, 44, 45, 47, 57, 66, 78, 79, 83, 87, 89, 92, 94, 96, 105–115, 125], DhlA [75, 76, 93, 97], DmbA [44, 89], DmlA [47], DpcA [38] and LinB [28, 44, 45, 47, 57, 61, 89, 95]. Abbreviations: BSA, bovine serum albumin; CB, 1‐chlorobutane, DCA; 1,2‐dichloroethane; DKR, dynamic kinetic resolution; KR, kinetic resolution; POI, protein of interest; TCP, 1,2,3‐trichloropropane; TEV, cleavage site for TEV protease.…”

Section: Applications Of Hldsmentioning

confidence: 99%

“…Detection of chemicals using biosensors provides a simple and rapid alternative to the traditional analytical techniques, such as gas and liquid chromatography, which are time‐consuming, expensive and not suitable for continuous measurements [92–95]. Initial attempts to construct biosensors for halogenated substrates (Supporting information, Table S6) led to a system with dehalogenating cells immobilized in polymer beads as a biological component and ion selective electrodes as a transducer [96, 97].…”

Section: Applications Of Hldsmentioning

confidence: 99%

“…The performance of the biosensor is critically influenced by the selection of an appropriate immobilization method for the biological component. The dehalogenating cells were encapsulated on the transducer [92–94, 96, 97], while the purified enzyme was covalently bound [95]. Two previous reports on covalent immobilization of HLDs described covalent binding of DhaA onto alumina support impregnated by polyethyleneimine [67] and combination of affinity and covalent binding of DhlA on iron oxide nanoparticles [99].…”

Section: Applications Of Hldsmentioning

confidence: 99%

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Haloalkane dehalogenases: Biotechnological applications

Koudeláková

Bidmanová

Dvořák

et al. 2012

Biotechnology Journal

138

120

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Haloalkane dehalogenases (EC 3.8.1.5, HLDs) are α/β-hydrolases which act to cleave carbon-halogen bonds. Due to their unique catalytic mechanism, broad substrate specificity and high robustness, the members of this enzyme family have been employed in several practical applications: (i) biocatalytic preparation of optically pure building-blocks for organic synthesis; (ii) recycling of by-products from chemical processes; (iii) bioremediation of toxic environmental pollutants; (iv) decontamination of warfare agents; (v) biosensing of environmental pollutants; and (vi) protein tagging for cell imaging and protein analysis. This review discusses the application of HLDs in the context of the biochemical properties of individual enzymes. Further extension of HLD uses within the field of biotechnology will require currently limiting factors - such as low expression, product inhibition, insufficient enzyme selectivity, low affinity and catalytic efficiency towards selected substrates, and instability in the presence of organic co-solvents - to be overcome. We propose that strategies based on protein engineering and isolation of novel HLDs from extremophilic microorganisms may offer solutions.

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Characteristics of a microbial assay for the detection of halogenated hydrocarbons using cells of an actinomycete‐like organism as a biological component

Peter

Buchinger

Karner

et al. 1997

Acta Biotechnologica

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Cells of an Actinomycete-like bacterium, strain GJ70, with the ability to degrade several haloalkanes were used as a biological component in a discontinuous microbial bioassay for the detection of 1,3-dichloropropene and 1.2-dibromoethane in wakr. The ceils were entrapped in different matrices such as calcium alginate, carrageenan, chitosan. polyacrylamide-hydrazide and chitosan-carboxymethyl cellulose; the specific dehalogenating activity of the immobilized cells was highest with the two last matrices. By the addition of small beads of immobilized cells to a stirred sample solution and by the use of an ion selective electrode (ISE) for the quantification of enzymatically released halogen ions, the concentration of halogenated hydrocarbons could be estimated by determining the change of electrode potential within a period of 5 min. The detection limits for 1,3-dichloropropene and 1,Zdibromoethane were below 100 pg/I and 25 pgA, respectively; the relative standard deviation was c 10%. In addition, several chlorinated and brominated hydrocarbons were converted by the bacterial cells at a reduced rate e.g. 1,2-dibromopropane, 1-bromoethane, 1,5-dichloropentane, etc. Moreover, temperatures of between 20 and 40 "C did not affect the enzymatic activity of the cells, and a pH of between at 5 and 9 had little influence. Several organic substances and non-metabolizable compounds did not affect the conversion, whereas some heavy metal ions acted as inhibitors.

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Development of a microbial bioassay for chlorinated and brominated hydrocarbons

Cited by 23 publications

References 12 publications

Enzymatic assays for the assessment of toxic effects of halogenated organic contaminants in water and food. A review

Enzymatic assays for the assessment of toxic effects of halogenated organic contaminants in water and food. A review

Haloalkane dehalogenases: Biotechnological applications

Characteristics of a microbial assay for the detection of halogenated hydrocarbons using cells of an actinomycete‐like organism as a biological component

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