Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.10.3.2 (laccase)
 4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Laccase (E.C. 1.10.3.2) is one of the well-studied enzymes used for bioremediation of xenobiotics such as phenols, anilines, etc. Its broad substrate specificity offers a wide opportunity for screening pollutants in order to predict potential targets for degradation. Present study utilizes protein-ligand docking as a tool to achieve the said. For virtual screening, a set of pollutants were selected from five different industries from EPA. X-ray crystal structures of laccase enzymes were taken from the Brookhaven Protein Data Bank (PDB). Two-dimensional structures of pollutants were downloaded from the NCBI Pubchem, which were further converted into three-dimensional structures using CORINA. Protein-ligand docking was carried out using GOLD. Nearly 30 and 17% of the selected datasets showed the best average GOLD fitness score for fungal and bacterial laccase enzyme respectively, suggesting thereby that laccase might be able to oxidize these pollutants. Moreover, in few cases like anthracene, phenanthrene, etc., there is experimental data to support this hypothesis. Similar kind of work would be helpful to find putative pollutants for other biodegradative enzymes.
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PMID:An in silico [correction of insilico] approach to bioremediation: laccase as a case study. 1760 96

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 PEG400 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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PMID:Laccase-catalyzed removal of diphenylamine from synthetic wastewater. 1902 27