Chlorhexidine (CHX) and octenidine (OCT), antimicrobial compounds used in oral care products (toothpastes and mouthwashes), were recently revealed to interfere with human sex hormone receptor pathways. Experiments employing model organisms-white-rot fungi Irpex lacteus and Pleurotus ostreatus-were carried out in order to investigate the biodegradability of these endocrine-disrupting compounds and the capability of the fungi and their extracellular enzyme apparatuses to biodegrade CHX and OCT. Up to 70% ± 6% of CHX was eliminated in comparison with a heat-killed control after 21 days of in vivo incubation. An additional in vitro experiment confirmed manganese-dependent peroxidase and laccase are partially responsible for the removal of CHX. Up to 48% ± 7% of OCT was removed in the same in vivo experiment, but the strong sorption of OCT on fungal biomass prevented a clear evaluation of the involvement of the fungi or extracellular enzymes. On the other hand, metabolites indicating the enzymatic transformation of both CHX and OCT were detected and their chemical structures were proposed by means of liquid chromatography-mass spectrometry. Complete biodegradation by the ligninolytic fungi was not achieved for any of the studied analytes, which emphasizes their recalcitrant character with low possibility to be removed from the environment.

• Keywords
• chlorhexidine, dental hygiene, laccase, ligninolytic fungi, manganese-dependent peroxidase, octenidine, personal care products, quaternary ammonium compounds, recalcitrant pollutant,
• MeSH
• Anti-Infective Agents, Local metabolism   MeSH
• Biodegradation, Environmental * MeSH
• Chlorhexidine chemistry   metabolism   MeSH
• Fungi metabolism   MeSH
• Imines MeSH
• Humans MeSH
• Metabolomics methods   MeSH
• Pyridines chemistry   metabolism   MeSH
• Dental Care MeSH
• Transformation, Genetic MeSH
• Check Tag
• Humans MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Anti-Infective Agents, Local MeSH
• Chlorhexidine MeSH
• Imines MeSH
• octenidine MeSH Browser
• Pyridines MeSH

White-rot fungi that are efficient lignin degraders responsible for its turnover in nature have appeared twice in the center of biotechnological research - first, when the lignin degradation process started being systematically investigated and major enzyme activities and mechanisms involved were described, and second, when the huge remediation potential of these organisms was established. Originally, Phanerochaete chrysosporium became a model organism, characterized by a secondary metabolism regulatory pattern triggered by nutrient (mostly nitrogen) limitation. Last decade brought evidence of more varied regulatory patterns in white-rot fungi when ligninolytic enzymes were also abundantly synthesized under conditions of nitrogen sufficiency. Gradually, research was focused on other species, among them Irpex lacteus showing a remarkable pollutant toxicity resistance and biodegradation efficiency. Systematic research has built up knowledge of biochemistry and biotechnological applicability of this fungus, stressing the need to critically summarize and estimate these scattered data. The review attempts to evaluate the information on I. lacteus focusing on various enzyme activities and bioremediation of organopollutants in water and soil environments, with the aim of mediating this knowledge to a broader microbiological audience.

• MeSH
• Basidiomycota enzymology   genetics   metabolism   MeSH
• Biodegradation, Environmental MeSH
• Biotechnology * MeSH
• Fungal Proteins genetics   metabolism   MeSH
• Environmental Pollutants metabolism   MeSH
• Lignin metabolism   MeSH
• Gene Expression Regulation, Fungal MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Review MeSH
• Names of Substances
• Fungal Proteins MeSH
• Environmental Pollutants MeSH
• Lignin MeSH

The wood-decomposing fungal species Antrodia macra, A. pulvinascens, Ceriporiopsis aneirina, C. resinascens and Dichomitus albidofuscus were determined for production of laccase (LAC), Mn peroxidase (MnP), lignin peroxidase (LiP), endo-l,4-P-beta-glucanase, endo-l,4-beta-xylanase, cellobiohydrolase, 1,4-beta-glucosidase and 1,4-beta-xylosidase. The results confirmed the brown-rot mode of Antrodia spp. which did not produce the activity of LAC and MnP. The remaining species performed detectable activity of both enzymes while no strain produced LiP. Significant inhibition of LAC production by high nitrogen was found in all white-rot species while only MnP of D. albidofuscus was regulated in the same way. The endoglucanase and endoxylanase activities of white-rotting species were inhibited by glucose in the medium while those of Antrodia spp. were not influenced by glucose concentration. The regulation of enzyme activity and bio-mass production can vary even within a single fungal genus.

• MeSH
• Basidiomycota enzymology   isolation & purification   metabolism   MeSH
• Wood microbiology   MeSH
• Nitrogen metabolism   MeSH
• Fungal Proteins metabolism   MeSH
• Laccase genetics   metabolism   MeSH
• Lignin metabolism   MeSH
• Peroxidases metabolism   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Nitrogen MeSH
• Fungal Proteins MeSH
• Laccase MeSH
• Lignin MeSH
• lignocellulose MeSH Browser
• manganese peroxidase MeSH Browser
• Peroxidases MeSH

Trametes pubescens and Pleurotus ostreatus, immobilized on polyurethane foam cubes in bioreactors, were used to decolorize three industrial and model dyes at concentrations of 200, 1000 and 2000 ppm. Five sequential cycles were run for each dye and fungus. The activity of laccase, Mn-dependent and independent peroxidases, lignin peroxidase, and aryl-alcohol oxidase were daily monitored during the cycles and the toxicity of media containing 1000 and 2000 ppm of each dye was assessed by the Lemna minor (duckweed) ecotoxicity test. Both fungi were able to efficiently decolorize all dyes even at the highest concentration, and the duckweed test showed a significant reduction (p < or = 0.05) of the toxicity after the decolorization treatment. T. pubescens enzyme activities varied greatly and no clear correlation between decolorization and enzyme activity was observed, while P. ostreatus showed constantly a high laccase activity during decolorization cycles. T. pubescens showed better decolorization and detoxication capability (compared to the better known P. ostreatus). As wide differences in enzyme activity of the individual strains were observed, the strong decolorization obtained with the two fungi suggested that different dye decolorization mechanisms might be involved.

• MeSH
• Coloring Agents metabolism   MeSH
• Biodegradation, Environmental MeSH
• Bioreactors microbiology   MeSH
• Fermentation MeSH
• Cells, Immobilized metabolism   MeSH
• Pleurotus enzymology   metabolism   MeSH
• Polyporales enzymology   metabolism   MeSH
• Industrial Microbiology * MeSH
• Industrial Waste * MeSH
• Textile Industry * MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Comparative Study MeSH
• Names of Substances
• Coloring Agents MeSH
• Industrial Waste * MeSH

Three new chromatographic forms of Dichomitus squalens manganese-dependent peroxidase (MnP) were isolated from wheat-straw cultures using Mono Q and connective interaction media (CIM) fast protein liquid chromatography. Enzymes revealed identical molar mass of 50 kDa (estimated by SDS-PAGE) and pI values of 3.5, however, they varied in Km values obtained for Mn2+ oxidation. The addition of wood and straw methanol extracts to the cultures showed that the production of MnPs in wheat-straw cultures was influenced rather by the type of cultivation than by phenolic compounds from lignocellulosic material which induced laccase production. The purified CIM1 MnP was able to decolorize selected azo and anthraquinone dyes more rapidly than laccase Lc1. In vitro dye decolorization showed a synergistic cooperation of MnP and laccase. In the case of CSB degradation MnP prevented from the production of a differently colored substance that could be produced after CSB degradation by laccase-HBT system.

• MeSH
• Anthraquinones metabolism   MeSH
• Azo Compounds metabolism   MeSH
• Bacterial Proteins isolation & purification   metabolism   MeSH
• Color MeSH
• Coloring Agents metabolism   MeSH
• Electrophoresis, Polyacrylamide Gel MeSH
• Laccase isolation & purification   metabolism   MeSH
• Lignin metabolism   MeSH
• Molecular Weight MeSH
• Mycology methods   MeSH
• Naphthalenesulfonates metabolism   MeSH
• Oxidation-Reduction MeSH
• Peroxidases isolation & purification   metabolism   MeSH
• Polyporaceae enzymology   MeSH
• Triticum MeSH
• Drug Synergism MeSH
• Trypan Blue metabolism   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Comparative Study MeSH
• Names of Substances
• Anthraquinones MeSH
• Azo Compounds MeSH
• Bacterial Proteins MeSH
• Coloring Agents MeSH
• C.I. Reactive Violet 5 MeSH Browser
• Laccase MeSH
• Lignin MeSH
• lignocellulose MeSH Browser
• manganese peroxidase MeSH Browser
• Naphthalenesulfonates MeSH
• Peroxidases MeSH
• pontamine sky blue MeSH Browser
• reactive orange 16 MeSH Browser
• Remazol Brilliant Blue R MeSH Browser
• Trypan Blue MeSH