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

Recent studies documented that several processes in filamentous fungi are connected with microsomal enzyme activities. In this work, microsomal subproteomes of Pleurotus ostreatus were analyzed by two-dimensional (2-D) polyacrylamide gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry analysis. To assess proteome dynamics, microsomal proteins were isolated from fungal cultures after 7 and 12 days of cultivation. Additionally, 10 mg/L of 17α-ethinylestradiol (EE2) was treated with the cultures during 2 days. Despite the EE2 degradation by the fungus reached 97 and 76.3 % in 7- and 12-day-old cultures, respectively, only a minor effect on the composition of microsomal proteins was observed. The changes in protein maps related to ageing prevailed over those induced by EE2. Epoxide hydrolase, known to metabolize EE2, was detected in 12-day-old cultures only which suggests differences in EE2 degradation pathways utilized by fungal cultures of different age. The majority (32 %) of identified microsomal proteins were parts of mitochondrial energy metabolism.

• MeSH
• Electrophoresis, Gel, Two-Dimensional MeSH
• Fungal Proteins analysis   MeSH
• Microsomes chemistry   MeSH
• Pleurotus chemistry   MeSH
• Proteome analysis   MeSH
• Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Fungal Proteins MeSH
• Proteome MeSH

Fungal, ligninolytic enzymes have attracted a great attention for their bioremediation capabilities. A deficient knowledge of regulation of enzyme production, however, hinders the use of ligninolytic fungi in bioremediation applications. In this work, a transcriptional analyses of laccase and manganese peroxidase (MnP) production by two white rots was combined with determination of pI of the enzymes and the evaluation of 17α-ethinyloestradiol (EE2) degradation to study regulation mechanisms used by fungi during EE2 degradation. In the cultures of Trametes versicolor the addition of EE2 caused an increase in laccase activity with a maximum of 34.2 ± 6.7 U g⁻¹ of dry mycelia that was observed after 2 days of cultivation. It corresponded to a 4.9 times higher transcription levels of a laccase-encoding gene (lacB) that were detected in the cultures at the same time. Simultaneously, pI values of the fungal laccases were altered in response to the EE2 treatment. Like T. versicolor, Irpex lacteus was also able to remove 10 mg l⁻¹ EE2 within 3 days of cultivation. While an increase to I. lacteus MnP activity and MnP gene transcription levels was observed at the later phase of the cultivation. It suggests another metabolic role of MnP but EE2 degradation.

• MeSH
• Ethinyl Estradiol metabolism   MeSH
• Fungal Proteins genetics   metabolism   MeSH
• Culture Media MeSH
• Laccase genetics   metabolism   MeSH
• Lignin metabolism   MeSH
• Mycelium metabolism   MeSH
• Peroxidases genetics   metabolism   MeSH
• Polyporales enzymology   genetics   growth & development   MeSH
• Industrial Microbiology methods   MeSH
• Gene Expression Regulation, Enzymologic * MeSH
• Gene Expression Regulation, Fungal MeSH
• Trametes enzymology   genetics   growth & development   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Ethinyl Estradiol MeSH
• Fungal Proteins MeSH
• Culture Media MeSH
• Laccase MeSH
• Lignin MeSH
• manganese peroxidase MeSH Browser
• Peroxidases MeSH