Adsorption of BSA Protein in Aqueous Medium Using Vegetable Tannin Resin from Acacia mearnsii (Mimosa) and Modified Lignocellulosic Fibers from the Bark of Eucalyptus citriodora.

Proteins are abundant biomolecules found in human cells, as well as pathogenic bacteria and viruses. Some of them become pollutants when released into water. Adsorption is an advantageous method for separating proteins in aqueous media since proteins are already immobilized on solid surfaces. Adsorbents with surfaces rich in tannins are efficient due to their affinity for strong interactions with the various amino acids that make up proteins. This work aimed to develop an adsorbent for protein adsorption in aqueous medium using lignocellulosic materials modified from eucalyptus bark and vegetable tannins. A more efficient resin was prepared containing 10% eucalyptus bark fibers and 90% tannin mimosa by condensation with formaldehyde, and it was characterized by UV-Vis, FTIR-ATR spectroscopy and determinations of degree of swelling, bulk and bulk density and specific mass. For UV-Vis spectroscopy the percentage of condensed and hydrolysable tannins in the extracts of fibers of the dry husks of Eucalyptus Citriodora was estimated and it was also determined your soluble solids. The study of bovine serum albumin (BSA) adsorption was carried out in batch with quantification by UV-Vis spectroscopy. The most efficient prepared resin obtained 71.6 ± 2.78% removal in a solution of 260 mg L-1 of BSA working in a better pH range of the aqueous solution of BSA in its isoelectric point, ~ 5, 32 ± 0.02, under these conditions, the synthesized resin can reach a maximum BSA adsorption capacity of ~ 26.7 ± 0.29 mg g-1 in 7 min. The new synthesized resin presents good prospects for adsorption of proteins or species that in their structure have higher percentages of amino functional groups or amino acids with aliphatic, acidic and/or basic hydrophilic characteristics.

Molecular Interactions of an Ornithine-Rich pH-Responsive Self- Assembling Peptide with a Model Lipid Membrane: Conformational Aspects.

Investigating interactions of designed peptide-based biomaterials with lipid membranes is important for applications in nanobiotechnology. Here the interaction of an ornithine-rich pH-responsive peptide called P11-5 with a model membrane was investigated employing Fourier transform infrared spectroscopy (FTIR). The results showed that in the range of pH 6.0-8.0 the peptide P11-5 shows spectral features which are evidence of the presence of peptides with antiparallel beta-sheet conformation (bands in the range 1625-1615 cm-1), as also spectral features which indicate the existence of random coil conformation (bands in the range 1640-1648 cm-1). Two types of membranes were used, 1,2- dipalmitoyl-sn-3-glycero-phosphocholine (DPPC) membranes with zwitterionic head groups and 1,2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt) (DPPG) membranes with anionic head groups. It was showed that there was a distinct peptide interaction under different pH values, pH 6.0, 7.0 and 8.0 for each type of lipid membrane with DPPC membrane preventing the peptide self-association even at basic pH, while for DPPG membrane there was a more evident peptide-lipid interaction. FTIR measurements indicate that in the presence of DPPC membrane the peptide was prevented to form beta-sheet aggregates at basic pH, while in the presence of DPPG membranes the self-association behavior of the peptide was more similar to its behavior when in aqueous solution in the absence of lipid membranes. Such results are important for the potential development of novel biomolecular nanostructured materials by the physico-chemical understanding of the peptide-lipid interactions.