The biosorption of mercury (II) on 14 fungal biomasses, Aspergillus flavus I–V, Aspergillus fumigatus I-II, Helminthosporium sp., Cladosporium sp., Mucor rouxii mutant, M. rouxii IM-80, Mucor sp 1 and 2, and Candida albicans, was studied in this work. It was found that the biomasses of the fungus M. rouxii IM-80, M. rouxii mutant, Mucor sp1, and Mucor sp 2 were very efficient removing the metal in solution, using dithizone, reaching the next percentage of removals: 95.3%, 88.7%, 80.4%, and 78.3%, respectively. The highest adsorption was obtained at pH 5.5, at 30°C after 24 hours of incubation, with 1 g/100 mL of fungal biomass.
The development of antifungal drugs that inhibit lanosterol 14-α-demethylase (CYP51) via non-covalent ligand interactions is a strategy that is gaining importance. A series of novel tetraindol-4-one derivatives with 1-and 2-(2,4-substituted phenyl) side chains were designed and synthesized based on the structure of CYP51 and fluconazole. The antifungal activities of these derivatives against eight human pathogenic filamentous fungi and yeast strains were evaluated in vitro by measuring the minimal inhibitory concentrations. Nearly all tested compounds 8a-g displayed activity against Candida tropicalis, Candida guilliermondii and Candida parapsilosis with a minimum inhibitory concentration (MIC) value until 8 µg mL 1 , on the other hand compounds 7a-g showed activity against Aspergillus fumigatus with a MIC value of 31.25 µg mL 1 . A molecular modeling study of the binding interactions between compounds 6, 7d, 8g and the active site of MtCYP51 was conducted based on the computational docking results.
A soluble alpha-glucosidase was partially purified from Candida albicans cells by a three-step procedure consisting of size-exclusion, ion-exchange and adsorption chromatographies. After the last step, enzyme was enriched about 8.7-fold with a yield of 13% over the starting material and analysis of the purified preparation revealed two major polypeptides of 36 and 47 kDa. The latter was responsible for enzyme activity as visualized with a fluorescent substrate. Nigerose, an alpha-1,3-linked glucose disaccharide, was preferentially hydrolyzed by the purified enzyme over other glucosedisaccharides bearing distinct alpha-linkages. The purified alpha-glucosidase also converted the GlcMan9GlcNAc2 oligosaccharide into the Man9GlcNAc2 product in a time-dependent manner. These and other determined properties are consistent with a type GII alpha-glucosidase probably involved in N-glycan processing.
A soluble alpha-glucosidase was partially purified from Candida albicans cells by a three-step procedure consisting of size-exclusion, ion-exchange and adsorption chromatographies. After the last step, enzyme was enriched about 8.7-fold with a yield of 13% over the starting material and analysis of the purified preparation revealed two major polypeptides of 36 and 47 kDa. The latter was responsible for enzyme activity as visualized with a fluorescent substrate. Nigerose, an alpha-1,3-linked glucose disaccharide, was preferentially hydrolyzed by the purified enzyme over other glucosedisaccharides bearing distinct alpha-linkages. The purified alpha-glucosidase also converted the GlcMan9GlcNAc2 oligosaccharide into the Man9GlcNAc2 product in a time-dependent manner. These and other determined properties are consistent with a type GII alpha-glucosidase probably involved in N-glycan processing.
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