Microalgal biofouling formation on tubular cellulose-ester membranes during dewatering by forward osmosis.

This work assesses the biofouling formation of a microalgal consortium, cultivated in wastewater, on dialysis tubular membranes with no supporting layer, in both batch and continuous FO dewatering modes. The biological adhesion strength was compared with the predictions from the Baier and Vogler biocompatibility theories, employing critical surface tension (γc) and water adhesion tension (τ0), respectively, as measurable parameters of surface wettability. The results indicate that most of the tested membranes presented amphiphilic surface characteristics (τ0=22 to 45 mJ.m-2, θW ≈ 65˚) with a minimal biological adhesion tendency, which is compatible with the Vogler criteria. However, the membrane exposed the longest time to the microalgal culture presented more hydrophobic characteristics and poor wettability. The existing thermodynamic models succeeded in predicting cell-cell and cell-surface interactions as a competitive phenomenon. Nevertheless, the XDLVO model was used to determine changes in the cell-to-surface attraction dynamics. This assessment of microalgal foulant-membrane interfacial interactions helps to enhance understanding of the fouling mechanisms present on a novel FO membrane surface.

pH-dependent structural conformations of B-phycoerythrin from Porphyridium cruentum.

B-phycoerythrin from the red alga Porphyridium cruentum was crystallized using the technique of capillary counter-diffusion. Crystals belonging to the space group R3 with almost identical unit cell constants and diffracting to 1.85 and 1.70 Å were obtained at pH values of 5 and 8, respectively. The most important difference between structures is the presence of the residue His88α in two different conformations at pH 8. This residue is placed next to the chromophore phycoerythrobilin PEB82α and the new conformation results in the relocation of the hydrogen-bond network and hydration around PEB82α, which probably contributes to the observed pH dependence of the optical spectrum associated with this chromophore. Comparison with the structures of B-phycoerythrin from other red algae shows differences in the conformation of the A-ring of the chromophore PEB139α. This conformational difference in B-phycoerythrin from P. cruentum enables the formation of several hydrogen bonds that connect PEB139α with the chromophore PEB158ß at the (αß)(3) hexamer association interface. The possible influence of these structural differences on the optical spectrum and the ability of the protein to perform energy transfer are discussed, with the two pH-dependent conformations of His88α and PEB82α being proposed as representing critical structural features that are correlated with the pH dependence of the optical spectrum and transient optical states during energy transfer.