Selective adsorption and recovery of precious metal ions using protein-rich biomass as efficient adsorbents

Various types of protein-rich biomass were examined as selective and environment-friendly adsorbents for precious metal ions. In the presence of base metal ions, Au³⁺, Pd²⁺ and Pt⁴⁺ ions were selectively adsorbed to samples of protein-rich biomass. Among the biomass samples tested, egg-shell membrane exhibited the highest adsorption ability and had high selectivity for Au, Pd and Pt ions. The maximum adsorption amount of Au, Pd and Pt ions to egg-shell membrane was approximately 250, 110 and 50 mg/g, respectively, in the presence of 0.1 M HCl. Microscopic observations and metal-ion desorption studies suggested that the precious metal ions were adsorbed and a portion of them was reduced to form metal nanoparticles on the egg-shell membrane, leading to high adsorption ratios. Investigations using glycoproteins indicated the importance of sugar chains in the adsorption of Au ions to the egg-shell membrane. Successful recovery of Au, Pd and Pt ions from industrial waste solutions was also demonstrated using egg-shell membrane. Biomass sheets (1 mm thick) made from egg-shell membrane also exhibited adsorption abilities for precious metal ions.     

In vivo biotinylation of recombinant beta-glucosidase enables simultaneous purification and immobilization on streptavidin coated magnetic particles

Beta-glucosidase from Bacillus licheniformis was in vivo biotinylated in Escherichia coli and subsequently immobilized directly from cell lysate on streptavidin coated magnetic particles. In vivo biotinylation was mediated by fusing the Biotin Acceptor Peptide to the C-terminal of beta-glucosidase and co-expressing the BirA biotin ligase. The approach enabled simultaneous purification and immobilization of the enzyme from crude cell lysate on magnetic particles because of the high affinity and strong interaction between biotin and streptavidin. After immobilization of the biotinylated beta-glucosidase the specific activity (using p-nitrophenyl-β-d-glucopyranoside as substrate) was increased 6.5 fold (compared to cell lysate). Immobilization of the enzyme resulted in improved thermal stability compared to free enzyme; after 2 h of incubation (at 50 °C) the residual enzyme activity of immobilized and free beta-glucosidase was 67 and 13%, respectively. The recyclability of immobilized beta-glucosidase was examined and it was observed that the enzyme could be recycled at least 9 times and retain 89% of its initial activity.