Removal of Copper from Water by Adsorption with Calcium-Alginate/Spent-Coffee-Grounds Composite Beads.

Calcium Alginate/Spent-Coffee-Grounds composite beads (CA-SCGs beads), which were made of two different proportions of alginate and spent-coffee-grounds (3:3 and 3:10), respectively, were used to adsorb Cu2+ in aqueous solution. These beads were compared with calcium alginate beads (CA beads) and spent-coffee-grounds (SCGs) in terms of adsorption capacity and rate of adsorption. The experiments were carried out at an initial pH of 4 at 30 °C with initial concentrations of Cu2+ from 10 ppm to 100 ppm. Equilibrium data was fitted with Langmuir, Freundlich and Sips models, and a pseudo-second-order kinetic equation. The Sips model showed the best correlation with the experimental values. CA-SCGs (3:3) beads showed a faster adsorption rate versus the CA beads. Also, CA-SCGs (3:3) beads showed a larger capacity of adsorption according to the Sips model, but not in the Langmuir model. FT-IR spectra and SEM images were taken for characterization. This study has shown that the CA-SCGs (3:3) beads have a synergistic effect, combining the capacity of adsorption of CA beads with the kinetics of the SCGs. The CA-SCGs beads have proven to be an effective adsorbent of Cu2+. Therefore, they can provide a use for the SCGs; which are considered pollutants in landfills.

Characterization of Recombinant His-Tag Protein Immobilized onto Functionalized Gold Nanoparticles.

The recombinant polyhistidine-tagged hemoglobin I ((His)6-rHbI) from the bivalve Lucina pectinata is an ideal biocomponent for a hydrogen sulfide (H2S) biosensor due to its high affinity for H2S. In this work, we immobilized (His)6-rHbI over a surface modified with gold nanoparticles functionalized with 3-mercaptopropionic acid complexed with nickel ion. The attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) analysis of the modified-gold electrode displays amide I and amide II bands characteristic of a primarily α-helix structure verifying the presence of (His)6-rHbI on the electrode surface. Also, X-ray photoelectron spectroscopy (XPS) results show a new peak after protein interaction corresponding to nitrogen and a calculated overlayer thickness of 5.3 nm. The functionality of the immobilized hemoprotein was established by direct current potential amperometry, using H2S as the analyte, validating its activity after immobilization. The current response to H2S concentrations was monitored over time giving a linear relationship from 30 to 700 nM with a corresponding sensitivity of 3.22 × 10-3 nA/nM. These results confirm that the analyzed gold nanostructured platform provides an efficient and strong link for polyhistidine-tag protein immobilization over gold and glassy carbon surfaces for a future biosensors development.