Laccase-mediated oxidation of natural glycosides

Baratto, Lara; Candido, Andrea; Marzorati, Mattia; Sagui, Francesca; Riva, Sergio; Danieli, Bruno

doi:10.1016/j.molcatb.2006.01.011

Cited by 52 publications

(27 citation statements)

References 11 publications

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“…Typical substrates for these enzymes are amines and phenols. These chemicals produce reactive radical intermediates after oxidation and these intermediates undergo chemical coupling to generate dimeric and oligomeric derivatives (Baratto et al, 2006). Removal of phenolic compounds using laccases has been studied (Torres et al, 2003) and it was found that polymers resulting from the laccase oxidation process were generally insoluble in water and could be removed by filtration or sedimentation.…”

Section: Use Of Enzyme In Wastewater Treatmentmentioning

confidence: 99%

Laccase‐Catalyzed Removal of Diphenylamine from Synthetic Wastewater

Saha

Taylor

Bewtra

et al. 2008

Water Environment Research

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The priority pollutant lists of both the U.S. Environmental Protection Agency (U.S. EPA) and the European Union (EU) include diphenylamine (DPA), a contaminant found in wastewater of various industries. This work demonstrates the potential of using enzymatic treatment to remove DPA from buffered synthetic wastewater. This treatment method includes oxidative polymerization of DPA using laccase from Trametes villosa, followed by removal of those polymers via adsorptive micellar flocculation (AMF) using sodium lauryl sulfate (SDS) and alum. Researchers investigated the effects of pH, laccase concentration, molecular mass, and concentration of polyethylene glycol (PEG) in continuously stirred batch reactors to achieve 95% substrate conversion in three hours. Treatment of 0.19 mM DPA was best at pH 7 and an enzyme concentration from 0.0025 to 0.0075 standard activity unit/mL. Except for PEG 400, optimum enzyme and PEG concentrations decreased with an increase in PEG molecular mass. Optimum AMF conditions were pH 3.0 to 6.5, 200 mg/L of SDS, and 150 mg/L of alum.

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Section: Use Of Enzyme In Wastewater Treatmentmentioning

confidence: 99%

Laccase‐Catalyzed Removal of Diphenylamine from Synthetic Wastewater

Saha

Taylor

Bewtra

et al. 2008

Water Environment Research

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“…[21,22] Briefly, HRP solution (11 mL, 1634 U, 0.33 mg mL À1 in 0.1 m phosphate buffer, pH 6) was treated with dry Eupergit C 250 L (200 mg) at room temperature or lower (5 8C) for 24 or 48 h, respectively ( Figure 1, step A). The residual oxyranyl groups of the resin were removed by treatment with a solution of ethanolamine (1.0 m) for 16 h (Figure 1, step B).…”

Section: Resultsmentioning

confidence: 99%

“…[21,22] At the end of the coupling period, the beads were collected by filtration, washed with H 2 O until no activity was detected in the washings and finally suspended in binding buffer. Before use, the beads were freeze-dried to remove the buffer.…”

Section: Determination Of Protein Concentrationmentioning

confidence: 99%

Selective Synthesis of DOPA and DOPA Peptides by Native and Immobilized Tyrosinase in Organic Solvent

et al. 2013

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Abstract3,4‐Dihydroxyphenylalanine (DOPA)‐containing peptides and proteins provide attractive design paradigms for pharmaceutical applications and engineering of synthetic polymers. An efficient and selective route to DOPA peptides by oxidation of L‐tyrosine derivatives with tyrosinase is reported. The efficiency of the procedure was tested by using successively recycled tyrosinase immobilized on Eupergit®C250L and coated with polyelectrolytes by the layer‐by‐layer method.

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“…OH groups of several glycosides can be oxidized by the laccase mediator system (LMS) of Trametes pubescens using TEMPO [4,20] or other components such as AZADO [30] Author contributions: Chih-Yu Cheng -author who participates in interpreting the data, drafting the article, revising it critically for important intellectual content. Chia-I.…”

Section: Introductionmentioning

confidence: 99%

Borate–fructose complex: A novel mediator for laccase and its new function for fructose determination

2015

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a b s t r a c tLaccase and borate-fructose complex were investigated by coincidence in a solid-state fermentation of Edenia sp. TS-76 under fructose oxidase screening. Laccase was purified to homogeneity with a 34-fold purification and 32% yield. Fructose had no significant effect on laccase activity, whereas borate reduced laccase activity by 60-90%; conversely, the borate-fructose complex increased laccase activity by nearly fourfold at pH 7.5. The complex caused a shift in the optimal pH for laccase from 5.0 to 7.5 and served as a highly efficient mediator. Borate complexed with fructose provides an alternative, time-saving, and specific method for serum fructose determination.

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Laccase-mediated oxidation of natural glycosides

Cited by 52 publications

References 11 publications

Laccase‐Catalyzed Removal of Diphenylamine from Synthetic Wastewater

Laccase‐Catalyzed Removal of Diphenylamine from Synthetic Wastewater

Selective Synthesis of DOPA and DOPA Peptides by Native and Immobilized Tyrosinase in Organic Solvent

Borate–fructose complex: A novel mediator for laccase and its new function for fructose determination

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