An enzymatic system for decolorization of wastewater dyes using immobilized CueO laccase‐like multicopper oxidase on poly‐3‐hydroxybutyrate

Bello-Gil, Daniel; Roig-Molina, Emma; Fonseca, Jennifer; Sarmiento-Ferrández, María Dolores; Ferrándiz, Marcela; Franco, Esther; Elena, María; Maestro, Beatríz; Sanz, Jesús M.

doi:10.1111/1751-7915.13287

Cited by 32 publications

(19 citation statements)

References 69 publications

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“…To validate MinP as an affinity tag, two enzymes, the ␤-galactosidase and the CueO oxidase from Escherichia coli, were genetically fused to minP by using the designed plasmid pSMinPN. Both enzymes are of wide applicability in the food industry for manufacturing lactosehydrolyzed products and the production of galactosylated products, in the case of the ␤-galactosidase (35), and for the textile and paper industries as well as for organic compound degradation with CueO oxidase (15,36). The ␤-galactosidase-coding gene was introduced by conventional cloning into XhoI and BamHI sites, resulting in the pSMinP-2 plasmid, and the cueO gene into XhoI and HindIII sites, resulting in the plasmid pSMinP-3.…”

Section: Resultsmentioning

confidence: 99%

“…Among GAPs, phasins constitute the most abundant group of proteins covering the granule (8,9) and have been widely used as anchoring tags to functionalize PHA supports for a variety of applications, such as affinity bioseparation (10), protein purification (11)(12)(13), enzyme immobilization (14)(15)(16), protein delivery to natural environments (17), diagnostics (18,19), cell targeting (20)(21)(22)(23)(24), and antimicrobials (25).…”

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confidence: 99%

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Dissecting the Polyhydroxyalkanoate-Binding Domain of the PhaF Phasin: Rational Design of a Minimized Affinity Tag

Mato

Blanco

Maestro

et al. 2020

Appl Environ Microbiol

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Phasin PhaF from Pseudomonas putida consists of a modular protein whose N-terminal domain (BioF) has been demonstrated to be responsible for binding to the polyhydroxyalkanoate (PHA) granule. BioF has been exploited for biotechnological purposes as an affinity tag in the functionalization of PHA beads with fusion proteins both in vivo and in vitro. The structural model of this domain suggests an amphipathic α-helical conformation with the hydrophobic residues facing the PHA granule. In this work, we analyzed the mean hydrophobicity and the hydrophobic moment of the native BioF tag to rationally design shorter versions that maintain affinity for the granule. Hybrid proteins containing the green fluorescent protein (GFP) fused to the BioF derivatives were studied for in vivo localization on PHA, stability on the surface of the PHA granule against pH, temperature, and ionic strength, and their possible influence on PHA synthesis. Based on the results obtained, a minimized BioF tag for PHA functionalization has been proposed (MinP) that retains similar binding properties but possesses an attractive biotechnological potential derived from its reduced size. The MinP tag was further validated by analyzing the functionality and stability of the fusion proteins MinP–β-galactosidase and MinP-CueO from Escherichia coli. IMPORTANCE Polyhydroxyalkanoates (PHAs) are biocompatible, nontoxic, and biodegradable biopolymers with exceptional applications in the industrial and medical fields. The complex structure of the PHA granule can be exploited as a toolbox to display molecules of interest on their surface. Phasins, the most abundant group of proteins on the granule, have been employed as anchoring tags to obtain functionalized PHA beads for high-affinity bioseparation, enzyme immobilization, diagnostics, or cell targeting. Here, a shorter module based on the previously designed BioF tag has been demonstrated to maintain the affinity for the PHA granule, with higher stability and similar functionalization efficiency. The use of a 67% shorter peptide, which maintains the binding properties of the entire protein, constitutes an advantage for the immobilization of recombinant proteins on the PHA surface both in vitro and in vivo.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Dissecting the Polyhydroxyalkanoate-Binding Domain of the PhaF Phasin: Rational Design of a Minimized Affinity Tag

Mato

Blanco

Maestro

et al. 2020

Appl Environ Microbiol

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“…The decolorization efficiency was 60%. Moreover, it was proven that the presence of other chemicals in wastewaters did not significantly affect the decolorization process [49]. As was shown by Khazravi et al [50], application of laccase immobilized onto oxidized, activated carbon could not only decolorized dye solution but also allowed the use of support material as a self-cleaning adsorbent.…”

Section: Removal Of Dyesmentioning

confidence: 91%

Enhanced Wastewater Treatment by Immobilized Enzymes

et al. 2021

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Purpose of Review In the presented review, we have summarized recent achievements on the use of immobilized oxidoreductases for biodegradation of hazardous organic pollutants including mainly dyes, pharmaceuticals, phenols, and bisphenols. In order to facilitate process optimization and achievement of high removal rates, effect of various process conditions on biodegradation has been highlighted and discussed. Recent Findings Current reports clearly show that immobilized oxidoreductases are capable of efficient conversion of organic pollutants, usually reaching over 90% of removal rate. Further, immobilized enzymes showed great recyclability potential, allowing their reuse in numerous of catalytic cycles. Summary Collected data clearly indicates immobilized oxidoreductases as an efficient biocatalytic tools for removal of hazardous phenolic compounds, making them a promising option for future water purification. Data shows, however, that both immobilization and biodegradation conditions affect conversion efficiency; therefore, process optimization is required to achieve high removal rates. Nevertheless, we have demonstrated future trends and highlighted several issues that have to be solved in the near-future research, to facilitate large-scale application of the immobilized oxidoreductases in wastewater treatment.

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“…Our results suggest that decolorization efficiency can be affected not only by the type of laccase, but also by the type of mediator, pH value, reaction temperature, and presence of other inhibitors in the reaction. The decolorization of industrial WWs by different laccase systems has been studied by Antosova et al (2018);Bello-Gil et al (2018) and Sondhi et al (2018); these studies have reported decolorization with up to 90% efficiency.…”

Section: Efficiencies Of Ww Decolorization and Detoxification Differ Among Laccases And Depend On Wastewater Propertiesmentioning

confidence: 99%

Decolorization and detoxification of textile wastewaters by recombinant Myceliophthora thermophila and Trametes trogii laccases

2018

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Laccases are multi-copper oxidoreductases with broad biotechnological applications. Here, we report detailed biochemical characterization of purified recombinant laccases originating from Myceliophthora thermophila (MtL) and Trametes trogii (TtL). We identified optimal conditions for decolorization of commercial dyes and textile wastewater samples. We also tested the toxicity of decolorized wastewater samples using human peripheral blood mononuclear cells. MtL and TtL were expressed in Saccharomyces cerevisiae, and secreted enzymes were purified by consecutive hydrophobic and gel chromatography. The molecular masses of TtL (~ 65 kDa) and MtL (> 100 kDa) suggested glycosylation of the recombinant enzymes. Deglycosylation of MtL and TtL led to 25% and 10% decreases in activity, respectively. In a thermal stability assay, TtL retained 61% and MtL 86% of the initial activity at 40 °C. While TtL retained roughly 50% activity at 60 °C, MtL lost stability at temperatures higher than 40 °C. MtL and TtL preferred syringaldazine as a substrate, and the catalytic efficiencies for ABTS oxidation were 7.5 times lower than for syringaldazine oxidation. In the presence of the mediator HBT, purified TtL almost completely decolorized dyes within 30 min and substantially decolorized wastewater samples from a textile factory (up to 74%) within 20 h. However, products of TtL-catalyzed decolorization were more toxic than MtL-decolorized products, which were almost completely detoxified.

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An enzymatic system for decolorization of wastewater dyes using immobilized CueO laccase‐like multicopper oxidase on poly‐3‐hydroxybutyrate

Cited by 32 publications

References 69 publications

Dissecting the Polyhydroxyalkanoate-Binding Domain of the PhaF Phasin: Rational Design of a Minimized Affinity Tag

Dissecting the Polyhydroxyalkanoate-Binding Domain of the PhaF Phasin: Rational Design of a Minimized Affinity Tag

Enhanced Wastewater Treatment by Immobilized Enzymes

Decolorization and detoxification of textile wastewaters by recombinant Myceliophthora thermophila and Trametes trogii laccases

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