Effect of Low Doses of Guaiacol and Ethanol on Enzymatic Activity of Fungal Cultures

The influence of low doses of guaiacol and ethanol, the natural effectors of lignin and phenolics transformations, on laccase and peroxidase activities produced by two strains of Basidiomycetes, Pleurotus sajor-caju and Trametes versicolor, was evaluated. Fungal mycelia were grown for 2 weeks on liquid media containing serial dilutions of guaiacol or ethanol ranging from 100−1 to 100−20 mol/L. Laccase and peroxidase activities in the medium were measured at the end of 2 weeks. The effect of low doses of guaiacol and ethanol on enzyme activities was manifested in an oscillating manner. Similar response patterns were observed when pure enzymes were exposed to the same serial dilutions of guaiacol and ethanol. T. versicolor cultures enriched with 40 mmol guaiacol (simulating natural environmental conditions) also displayed oscillating enzyme activity patterns in response to serial dilutions of guaiacol, but the maximum enzyme activity values were increased compared to those observed in cultures not receiving 40 mmol guaiacol. The differences between maxima and minima varied among the experimental groups and depended on the species of fungus, type of effector, and kind of enzyme. The results suggests the possibility of subtle regulation of enzymatic activity on the molecular level

The Influence of Very Low Doses of Cisplatin on Tumor Cell Proliferation In Vitro and on Some Hematological and Enzymatic Parameters of Healthy Rats

Healthy rats had been treated for 2 or 6 weeks with 1.0 mL of 10-8 and 10-16 mg/mL of cisplatin. After 2 weeks of treatment, a significant increase in leukocyte and erythrocyte count and also in hematocrit was observed. Among leukocytes the number of neutrophils and eosinophils significantly increased. Biochemical analyses indicated a decrease in the glycogen content in the liver and kidneys after 2 weeks of treatment with low doses of cisplatin but at the end of the experiment (8th week of experiment) the stores of glycogen increased significantly. Biochemical analyses concerning the activity of some enzymes in the liver revealed a significant increase of peroxidase and acid phosphatase as well as catalase activities after 2 weeks of treatment. However, catalase was induced by a very low concentration of cisplatin, 10-16 mg/mL. After the cessation of cisplatin treatment the activity of enzymes returned to normal values. Human lung carcinoma cell line A549 (ECACC No 86012804) was also studied after treatment with the same doses of cisplatin and inhibition of its growth was observed. The results of these experiments strongly indicated that low doses of cisplatin could be stimulating for healthy cells but cytostatic for tumor cells. Possible mechanisms involved in the biological activity of very low cisplatin concentrations are discussed

Influence of very low doses of mediators on fungal laccase activity - nonlinearity beyond imagination

Laccase, an enzyme responsible for aerobic transformations of natural phenolics, in industrial applications requires the presence of low-molecular substances known as mediators, which accelerate oxidation processes. However, the use of mediators is limited by their toxicity and the high costs of exploitation. The activation of extracellular laccase in growing fungal culture with highly diluted mediators, ABTS and HBT is described. Two high laccase-producing fungal strains, Trametes versicolor and Cerrena unicolor, were used in this study as a source of enzyme. Selected dilutions of the mediators significantly increased the activity of extracellular laccase during 14 days of cultivation what was distinctly visible in PAGE technique and in colorimetric tests. The same mediator dilutions increased demethylation properties of laccase, which was demonstrated during incubation of enzyme with veratric acid. It was established that the activation effect was assigned to specific dilutions of mediators. Our dose-response dilution process smoothly passes into the range of action of homeopathic dilutions and is of interest for homeopaths

Synthesis and structural characterization of a novel phenoxazinone dye by use of a fungal laccase

Laccase, isolated from Cerrena unicolor, is able to transform 3-amino-4-hydroxybenzensulfonic acid into a water soluble phenoxazine dye with an extinction coefficient (epsilon) of 8600 M-1 cm(-1). The dye has been characterized using a variety of different analytic and spectroscopic techniques like UV-vis spectroscopy, HPLC (High Performance Liquid Chromatography), ESI/MS (Electrospray Ionization Mass Spectrometry) and the following NMR experiments: H-1, C-13, TOCSY (Total Correlation Spectroscopy), HSQC (Heteronuclear Single Quantum Coherence). HMBC (Heteronuclear Multiple Bond Coherence) showing the structure of 2-amino-3-oxo-3H-phenoxazine-8-sulfonic acid. The advantages of the presented biocatalytic system, in alignment with chemical system to obtain Curie_22, are eco-sustainability and one step performance. (C) 2010 Elsevier B.V. All rights reserved

Removal of Chlorophenols by Fungal Laccase in the Presence of Aromatic Alcohols

The effect of aromatic alcohols, coniferyl, sinapyl, vanillyl and iso-vanillyl alcohols, on the removal of chlorinated phenols from water environment by fungal laccases from Cerrena unicolor and Rhizoctonia praticola was studied. In optimal conditions all tested alcohols removed about 30 to 60% of chlorophenols from the supernatant, compared to that of laccase alone. R. praticola at pH 7.0 significantly removed more chlorophenols from supernatant than in the case of C. unicolor at pH 5.5. The laccase reaction is independent on the enzyme source and favours higher pH condition. Tested chlorophenols were partly coupled with aromatic alcohols and sedimented. It almost linearly depended on amounts of chlorine atoms in chlorophenols; more chlorine atoms resulted in higher yield of coupling reaction

Removal of Chlorophenols by Fungal Laccase in the Presence of Aromatic Alcohols

The effect of aromatic alcohols, coniferyl, sinapyl, vanillyl and iso-vanillyl alcohols, on the removal of chlorinated phenols from water environment by fungal laccases from Cerrena unicolor and Rhizoctonia praticola was studied. In optimal conditions all tested alcohols removed about 30 to 60% of chlorophenols from the supernatant, compared to that of laccase alone. R. praticola at pH 7.0 significantly removed more chlorophenols from supernatant than in the case of C. unicolor at pH 5.5. The laccase reaction is independent on the enzyme source and favours higher pH condition. Tested chlorophenols were partly coupled with aromatic alcohols and sedimented. It almost linearly depended on amounts of chlorine atoms in chlorophenols; more chlorine atoms resulted in higher yield of coupling reaction