Combined cross-linked enzyme aggregates from versatile peroxidase and glucose oxidase: Production, partial characterization and application for the elimination of endocrine disruptors

Taboada-Puig, Roberto; Junghanns, Charles; Demarche, Philippe; Moreira, Marı́a Teresa; Lema, Juan M.; Agathos, Spiros N.

doi:10.1016/j.biortech.2011.03.018

Cited by 109 publications

(69 citation statements)

References 34 publications

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“…Therefore, a range of in situ H 2 O 2 generation methods have been proposed, [22][23][24] which might be useful also for peroxidase-initiated polymerizations. Indeed Uyama et al and others reported a bienzymatic system for the polymerization of phenols comprising peroxidase as the initiation catalyst and glucose oxidase as in situ H 2 O 2 generation catalyst ( Figure 3) [25,26].…”

Section: Figurementioning

confidence: 99%

Enzyme Initiated Radical Polymerizations

2012

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Section: Figurementioning

confidence: 99%

Enzyme Initiated Radical Polymerizations

2012

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“…The estrogenic activity was measured by the LYES (lyticase yeast estrogen screen-assay assisted by enzymatic digestion) assay previously described by Taboada-Puig et al (2011), adapted from Schultis and Metzger (2004). The recombinant yeast Saccharomyces cerevisiae was kindly provided by the Laboratory of Microbial Ecology and Technology (Labmet, Ghent University, Belgium).…”

Section: Evaluation Of Estrogenic Activitymentioning

confidence: 99%

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

et al. 2011

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Laccase from Myceliophthora thermophila was covalently immobilised on Eupergit C and Eupergit C 250L yielding specific activities of up to 17 and 80 U/g, respectively. Due to its superior activity, Eupergit C 250L was chosen for further research. The somewhat lower catalytic efficiency (based on the ratio between the turnover number and the Michaelis constant, k cat /K M ) of the immobilised enzyme in comparison with that of the free enzyme was balanced by its increased stability and broader operational window related to temperature and pH. The feasibility of the immobilised laccase was tested by using a packed bed reactor (PBR) operating in consecutive cycles for the removal of Acid Green 27 dye as model substrate. High degrees of elimination were achieved (88, 79, 69 and 57% in 4 consecutive cycles), while the levels of adsorption on the support varied from 18 to 6%, proving that dye removal took place mainly due to the action of the enzyme. Finally, a continuous PBR with the solid biocatalyst was applied for the treatment of a solution containing the following endocrine disrupting chemicals: estrone (E1), 17b-estradiol (E2) and 17a-ethinylestradiol (EE2). At steady-state operation, E1 was degraded by 65% and E2 and EE2 were removed up to 80% and only limited adsorption of these compounds on the support, between 12 and 22%, was detected. In addition, a 79% decrease in estrogenic activity was detected in the effluent of the enzymatic reactor while only 14% was attained by inactivated laccase.

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“…In fact, the treatment of NP by MnP and VP was reported to reduce or even completely remove its estrogenic activity when treating NP at concentrations in the range of 45 μM [14] and 900 μM [16]. In this sense, the reduction of the estrogenicity after the treatment with Mn 3+ -malonate was attempted by using the LYES-assay (yeast estrogen screen-assay assisted by enzymatic digestion with lyticase) [14]. However, we did not obtain any concluding result, probably due to the insufficient sensitivity of the method at the low concentration of NP used.…”

Section: Resultsmentioning

confidence: 99%

“…In this regard, the capabilities of laccase, manganese peroxidase (MnP), and versatile peroxidase (VP) for NP removal at concentrations much higher than those found in the environment have been demonstrated [13,14]. Moreover, the results widely vary depending on the type and source of the enzyme, and furthermore, environmental conditions strongly influence the efficiency of the degradation process [15].…”

Section: Introductionmentioning

confidence: 99%

Continuous Removal of Nonylphenol by Versatile Peroxidase in a Two-Stage Membrane Bioreactor

Hernández

Eibes

Arca-Ramos

et al. 2015

Appl Biochem Biotechnol

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The ligninolytic enzymes versatile peroxidase (VP) and manganese peroxidase (MnP) have been previously described as efficient oxidizers of the endocrine disrupting chemical (EDC) nonylphenol at high concentrations of the pollutant. Envisaging the application of an enzymatic technology as a tertiary treatment in wastewater treatment plants, it is important to design a continuous reactor that performs the efficient removal of nonylphenol under environmental conditions. In the present research, a two-stage membrane bioreactor based on the production and use of Mn(3+)-malonate (chemical oxidant) was applied. The bioreactor consisted of an enzymatic reactor (R1) for the production of Mn(3+)-malonate by VP, coupled to an oxidation reactor (R2), where the oxidation of nonylphenol by Mn(3+)-malonate took place. The production of Mn(3+)-malonate in R1 was maintained constant: 500-700 μM with minimal deactivation of the enzyme. The oxidation reactor attained nearly complete removal of nonylphenol, even at a hydraulic retention time (HRT) shorter than 20 min. The operation with real wastewater containing nonylphenol at environmental concentrations (454 nM) was also successful, with a nonylphenol removal of 99.5% at a rate of 0.73 μM h(-1). Moreover, when the HRT of R2 was sharply reduced to 6.8 and 3.6 min, the removal of nonylphenol was maintained beyond 99%, which proves the feasibility of the system to remove the target compound present in a real effluent, even at very short HRTs.

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Combined cross-linked enzyme aggregates from versatile peroxidase and glucose oxidase: Production, partial characterization and application for the elimination of endocrine disruptors

Cited by 109 publications

References 34 publications

Enzyme Initiated Radical Polymerizations

Enzyme Initiated Radical Polymerizations

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

Continuous Removal of Nonylphenol by Versatile Peroxidase in a Two-Stage Membrane Bioreactor

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