Four marine-derived fungi for bioremediation of raw textile mill effluents

Textile dye effluents pose environmental hazards because of color and toxicity. Bioremediation of these has been widely attempted. However, their widely differing characteristics and high salt contents have required application of different microorganisms and high dilutions. We report here decolorization and detoxification of two raw textile effluents, with extreme variations in their pH and dye composition, used at 20–90% concentrations by each of the four marine-derived fungi. Textile effluent A (TEA) contained an azo dye and had a pH of 8.9 and textile effluent B (TEB) with a pH of 2.5 contained a mixture of eight reactive dyes. The fungi isolated from mangroves and identified by 18S and ITS sequencing corresponded to two ascomycetes and two basidiomycetes. Each of these fungi decolorized TEA by 30–60% and TEB by 33–80% used at 20–90% concentrations and salinity of 15 ppt within 6 days. This was accompanied by two to threefold reduction in toxicity as measured by LC₅₀ values against Artemia larvae and 70–80% reduction in chemical oxygen demand and total phenolics. Mass spectrometric scan of effluents after fungal treatment revealed degradation of most of the components. The ascomycetes appeared to remove color primarily by adsorption, whereas laccase played a major role in decolorization by basidiomycetes. A process consisting of a combination of sorption by fungal biomass of an ascomycete and biodegradation by laccase from a basidiomycete was used in two separate steps or simultaneously for bioremediation of these two effluents.     

Sensitivity of corneal biomechanical and optical behavior to material parameters using design of experiments method

The optical performance of the human cornea under intraocular pressure (IOP) is the result of complex material properties and their interactions. The measurement of the numerous material parameters that define this material behavior may be key in the refinement of patient-specific models. The goal of this study was to investigate the relative contribution of these parameters to the biomechanical and optical responses of human cornea predicted by a widely accepted anisotropic hyperelastic finite element model, with regional variations in the alignment of fibers. Design of experiments methods were used to quantify the relative importance of material properties including matrix stiffness, fiber stiffness, fiber nonlinearity and fiber dispersion under physiological IOP. Our sensitivity results showed that corneal apical displacement was influenced nearly evenly by matrix stiffness, fiber stiffness and nonlinearity. However, the variations in corneal optical aberrations (refractive power and spherical aberration) were primarily dependent on the value of the matrix stiffness. The optical aberrations predicted by variations in this material parameter were sufficiently large to predict clinically important changes in retinal image quality. Therefore, well-characterized individual variations in matrix stiffness could be critical in cornea modeling in order to reliably predict optical behavior under different IOPs or after corneal surgery.     

First structural evidence for the mode of diffusion of aromatic ligands and ligand-induced closure of the hydrophobic channel in heme peroxidases

The mode of binding of aromatic ligands in the substrate binding site on the distal heme side in heme peroxidases is well understood. However, the mode of diffusion through the extended hydrophobic channel and the regulatory role of the channel are not yet clear. To provide answers to these questions, the crystal structure of the complex of lactoperoxidase and 3-amino-1,2,4-triazole (amitrole) has been determined, which revealed the presence of two ligand molecules, one in the substrate binding site and the second in the hydrophobic channel. The binding of ligand in the channel induced a remarkable conformational change in the side chain of Phe254, which flips from its original distant position to interact with the trapped ligand in the hydrophobic channel. As a result, the channel is completely blocked so that no ligand can diffuse through it to the substrate binding site. Another amitrole molecule is bound to lactoperoxidase in the substrate binding site by replacing three water molecules, including the crucial iron-bound water molecule, W1. In this arrangement, the amino nitrogen atom of amitrole occupies the position of W1 and interacts directly with ferric iron. As a consequence, it prevents the binding of H₂O₂ to heme iron. Thus, the interactions of amitrole with lactoperoxidase obstruct both the passage of ligands through the hydrophobic channel as well as the binding of H₂O₂. This explains the amitrole toxicity. From binding studies, the dissociation constant (K _d) for amitrole with lactoperoxidase was found to be approximately 5.5 × 10⁻⁷ M, indicating high affinity.