“…S5), while longer incubation times allowed appreciable decolorizing efficiencies (reaching almost 100% for IC, Figs and ), resulting in improvements from 1.1‐fold (IC) to 1.4‐fold (RB5) and 1.7‐fold (NC) compared to the soluble protein. In particular, immobilized CueO‐mediated degradation of IC at neutral pH reached levels around 90% after 4 h, appreciably higher than those previously reported at pH 4.5 (7%) (Britos and Trelles, ). A striking case was methyl orange (MO), which was not degraded at all either by the soluble or immobilized enzyme in the tested conditions (data not shown).…”
Section: Resultsmentioning
confidence: 97%
“…on this substrate in the absence of mediators, that has been explained in terms of the lack of hydroxyl substituents in the molecule that would help promoting oxidation, leading to a very high redox potential (Pardo et al ., ). Nevertheless, a somewhat higher degradation of MO has been reported to occur at more acidic pH values (Britos and Trelles, ).…”
Section: Resultsmentioning
confidence: 99%
“…Although many oxidases from bacterial or fungal origin might possess better biotechnological properties in certain cases (Wesenberg et al ., ; Rodriguez Couto and Toca Herrera, ; Giardina et al ., ; Majeau et al ., ), we chose the CueO multicopper oxidase to establish the present proof‐of‐concept since this enzyme has already been thoroughly characterized both structurally and functionally for the oxidation of several organic substrates, including dyes (Zeng et al ., ; Britos and Trelles, ; Ma et al ., )…”
Section: Resultsmentioning
confidence: 99%
“…Enzymatic parameters of the hybrid BioF-CueO protein Although many oxidases from bacterial or fungal origin might possess better biotechnological properties in certain cases (Wesenberg et al, 2003;Rodriguez Couto and Toca Herrera, 2006;Giardina et al, 2010;Majeau et al, 2010), we chose the CueO multicopper oxidase to establish the present proof-of-concept since this enzyme has already been thoroughly characterized both structurally and functionally for the oxidation of several organic substrates, including dyes (Zeng et al, 2011;Britos and Trelles, 2016;Ma et al, 2017) To ensure a strong and specific adsorption of the CueO oxidase to PHB, a chimeric protein was constructed containing the BioF tag fused to the N-terminal of the CueO enzyme (Fig. S1).…”
Section: Resultsmentioning
confidence: 99%
“…A few studies have previously analysed the scope of substrates able to be oxidized by CueO (Kataoka et al, 2007;Li et al, 2007;Zeng et al, 2011), but have only recently included dye molecules (Britos and Trelles, 2016;Ma et al, 2017). Therefore, we aimed to study the activity of PHB-immobilized CueO on some representative dyes that were chosen to cover different structural families ( Fig.…”
Section: Substrate Range Of Immobilized Biof-cueomentioning
SummaryThe presence of synthetic dyes in wastewaters generated by the textile industry constitutes a serious environmental and health problem that urges the scientific community on an appropriate action. As a proof‐of‐concept, we have developed a novel approach to design enzymatic bioreactors with the ability to decolorize dye solutions through the immobilization of the bacterial CueO laccase‐like multicopper oxidase from Escherichia coli on polyhydroxybutyrate (PHB) beads by making use of the BioF affinity tag. The decolorization efficiency of the system was characterized by a series of parameters, namely maximum enzyme adsorption capacity, pH profile, kinetic constants, substrate range, temperature and bioreactor recycling. Depending on the tested dye, immobilization increased the catalytic activity of CueO by up to 40‐fold with respect to the soluble enzyme, reaching decolorization efficiencies of 45–90%. Our results indicate that oxidase bioreactors based on polyhydroxyalkanoates are a promising alternative for the treatment of coloured industrial wastewaters.
“…S5), while longer incubation times allowed appreciable decolorizing efficiencies (reaching almost 100% for IC, Figs and ), resulting in improvements from 1.1‐fold (IC) to 1.4‐fold (RB5) and 1.7‐fold (NC) compared to the soluble protein. In particular, immobilized CueO‐mediated degradation of IC at neutral pH reached levels around 90% after 4 h, appreciably higher than those previously reported at pH 4.5 (7%) (Britos and Trelles, ). A striking case was methyl orange (MO), which was not degraded at all either by the soluble or immobilized enzyme in the tested conditions (data not shown).…”
Section: Resultsmentioning
confidence: 97%
“…on this substrate in the absence of mediators, that has been explained in terms of the lack of hydroxyl substituents in the molecule that would help promoting oxidation, leading to a very high redox potential (Pardo et al ., ). Nevertheless, a somewhat higher degradation of MO has been reported to occur at more acidic pH values (Britos and Trelles, ).…”
Section: Resultsmentioning
confidence: 99%
“…Although many oxidases from bacterial or fungal origin might possess better biotechnological properties in certain cases (Wesenberg et al ., ; Rodriguez Couto and Toca Herrera, ; Giardina et al ., ; Majeau et al ., ), we chose the CueO multicopper oxidase to establish the present proof‐of‐concept since this enzyme has already been thoroughly characterized both structurally and functionally for the oxidation of several organic substrates, including dyes (Zeng et al ., ; Britos and Trelles, ; Ma et al ., )…”
Section: Resultsmentioning
confidence: 99%
“…Enzymatic parameters of the hybrid BioF-CueO protein Although many oxidases from bacterial or fungal origin might possess better biotechnological properties in certain cases (Wesenberg et al, 2003;Rodriguez Couto and Toca Herrera, 2006;Giardina et al, 2010;Majeau et al, 2010), we chose the CueO multicopper oxidase to establish the present proof-of-concept since this enzyme has already been thoroughly characterized both structurally and functionally for the oxidation of several organic substrates, including dyes (Zeng et al, 2011;Britos and Trelles, 2016;Ma et al, 2017) To ensure a strong and specific adsorption of the CueO oxidase to PHB, a chimeric protein was constructed containing the BioF tag fused to the N-terminal of the CueO enzyme (Fig. S1).…”
Section: Resultsmentioning
confidence: 99%
“…A few studies have previously analysed the scope of substrates able to be oxidized by CueO (Kataoka et al, 2007;Li et al, 2007;Zeng et al, 2011), but have only recently included dye molecules (Britos and Trelles, 2016;Ma et al, 2017). Therefore, we aimed to study the activity of PHB-immobilized CueO on some representative dyes that were chosen to cover different structural families ( Fig.…”
Section: Substrate Range Of Immobilized Biof-cueomentioning
SummaryThe presence of synthetic dyes in wastewaters generated by the textile industry constitutes a serious environmental and health problem that urges the scientific community on an appropriate action. As a proof‐of‐concept, we have developed a novel approach to design enzymatic bioreactors with the ability to decolorize dye solutions through the immobilization of the bacterial CueO laccase‐like multicopper oxidase from Escherichia coli on polyhydroxybutyrate (PHB) beads by making use of the BioF affinity tag. The decolorization efficiency of the system was characterized by a series of parameters, namely maximum enzyme adsorption capacity, pH profile, kinetic constants, substrate range, temperature and bioreactor recycling. Depending on the tested dye, immobilization increased the catalytic activity of CueO by up to 40‐fold with respect to the soluble enzyme, reaching decolorization efficiencies of 45–90%. Our results indicate that oxidase bioreactors based on polyhydroxyalkanoates are a promising alternative for the treatment of coloured industrial wastewaters.
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