No abstract

A number of anaerobic and aerobic bacterial species are known to decolourise azo dyes through the reduction of the azo bonds, forming the corresponding amines. In this work, we describe improved decolourisation conditions for model azo dyes by the ascomycete yeast Candida zeylanoides. The dyes were derived from the diazonium salts of metanilic and sulfanilic acids and N,N-dimethylaniline or 2-naphthol as coupling components. Total decolourisation times observed in culture media supplemented with 0.2mM dye ranged from 40 go 60 hours. The initial decolourisation rates were 14-52μmol.(g dry cell) -1 .h -1 , depending on dye structure. In the course of decolourisation either metanilic acid or sulfanilic acid were detected in the supernatant fluid, showing that decolourization by this yeast strain is due to azo bond reduction. None of those aminobenzenesulphonates supported microorganism growth as carbon and energy source but both could be used, to a limited extent, as nitrogen sources. The azo reductase activity is not significantly affected by pre-adaptation of the microorganism to the dyes.

No abstract

The commercial azo dye C.I. Reactive Orange 4 in its reactive and hydrolysed forms can be efficiently photodegraded, using commercial samples of TiO 2 as a photocatalyst. With UV light, aqueous solutions containing only dye and no dyebath additives are decolorised slightly more rapidly with Riedel-de-Häen TiO 2 than with Degussa P-25 TiO 2. The rate of decolorisation increases markedly with increasing pH. Sunlight is also very effective as a light source. On the other hand, comparison experiments involving UV irradiation of hydrolysed and unhydrolysed Reactive Orange 4 in a simulated spent dyebath showed Degussa P-25 TiO 2 to be significantly the more efficient catalyst, giving more than 90% decolorisation after 20 minutes.

Tacrine is an acetylcholinesterase (AChE) inhibitor used as a cognitive enhancer in the treatment of Alzheimer's disease (AD). However, its low therapeutic efficiency and a high incidence of side effects have limited its clinical use. In this study, the molecular mechanisms underlying the impact on brain activity of tacrine and two novel tacrine analogues (T1, T2) were approached by focusing on three aspects: (i) their effects on brain cholinesterase activity; (ii) perturbations on electron transport chain enzymes activities of non-synaptic brain mitochondria; and (iii) the role of mitochondrial lipidome changes induced by these compounds on mitochondrial bioenergetics. Brain effects were evaluated 18 h after the administration of a single dose (75.6 lmol/kg) of tacrine or tacrine analogues. The three compounds promoted a significant reduction in brain AChE and butyrylcholinesterase (BuChE) activities. Additionally, tacrine was shown to be more efficient in brain AChE inhibition than T2 tacrine analogue and less active than T1 tacrine analogue, whereas BuChE inhibition followed the order: T1 > T2 > tacrine. The studies using non-synaptic brain mitochondria show that all the compounds studied disturbed brain mitochondrial bioenergetics mainly via the inhibition of complex I activity. Furthermore, the activity of complex IV is also affected by tacrine and T1 treatments while FoF 1 -ATPase is only affected by tacrine. Therefore, the compounds' toxicity as regards brain mitochondria, which follows the order: tacrine >> T1 > T2, does not correlate with their ability to inhibit brain cholinesterase enzymes. Lipidomics approaches show that phosphatidylethanolamine (PE) is the most abundant phospholipids (PL) class in non-synaptic brain mitochondria and cardiolipin (CL) present the greatest diversity of molecular species. Tacrine induced significant perturbations in the mitochondrial PL profile, which were detected by means of changes in the relative abundance of phosphatidylcholine (PC), PE, phosphatidylinositol (PI) and CL and by the presence of oxidized phosphatidylserines. Additionally, in both the T1 and T2 groups, the lipid content and molecular composition of brain mitochondria PL are perturbed to a lesser extent than in the tacrine group. Abnormalities in CL content and the amount of oxidized phosphatidylserines were associated with significant reductions in mitochondrial enzymes activities, mainly complex I. These results indicate that tacrine and its analogues impair mitochondrial function and bioenergetics, thus compromising the activity of brain cells.