Addressing the issue of surface mechanisms and competitive effects in Cr(VI) reductive-adsorption on tin-hydroxyapatite in the presence of co-ions.

Our group recently proposed an innovative sustainable reductant-adsorbent material, tin(II)-hydroxyapatite (Sn/HAP, ca. 10 wt% Sn) for the interfacial Cr(VI) reductive adsorption process. In this study, Cr(VI) removal capacity was evaluated in multi-component solutions containing representative background ions (i.e., CaCl2, Ca(NO3)2, MgSO4, Na2SO4, Fe(NO3)3, AlCl3, Zn(NO3)2, or Mn(NO3)2). Sn/HAP was able to reduce Cr(VI) with complete Cr3+ adsorption on HAP surface, except in the presence of Fe3+ and Al3+ ions. Some metal ions co-existing in solution, such as Fe3+, Al3+, Zn2+, and Mn2+, were also adsorbed on HAP surface. Reuse experiments of the Sn/HAP sample, up to 7 runs, resulted in a total amount of reduced Cr(VI) of ca. 15-18 mg g-1. Fast kinetics of Cr(VI) reductive adsorption at 25 °C in a multi-metal component solution was observed. The pseudo-second order model was in excellent agreement with the experimental kinetic data, leading to a rate constant (k25°C) value of ca. 30 M-1 s-1. The collection of adsorption isotherms of Cr3+ and Fe3+, together with TEM-EDX analysis permitted the unveiling of competitive adsorption phenomena between metal ions. The obtained results demonstrate that Sn/HAP could be an efficient material for the removal of hexavalent chromium in aqueous solutions containing high concentrations of inorganic impurities.

Sustainable soy protein microsponges for efficient removal of lead (II) from aqueous environments.

Protein-based materials recently emerged as good candidates for water cleaning applications, due to the large availability of the constituent material, their biocompatibility and the ease of preparation. In this work, new adsorbent biomaterials were created from Soy Protein Isolate (SPI) in aqueous solution using a simple environmentally friendly procedure. Protein microsponge-like structures were produced and characterized by means of spectroscopy and fluorescence microscopy methods. The efficiency of these structures in removing Pb2+ ions from aqueous solutions was evaluated by investigating the adsorption mechanisms. The molecular structure and, consequently, the physico-chemical properties of these aggregates can be readily tuned by selecting the pH of the solution during production. In particular, the presence of ß-structures typical of amyloids as well as an environment characterized by a lower dielectric constant seem to enhance metal binding affinity revealing that hydrophobicity and water accessibility of the material are key features affecting the adsorption efficiency. Presented results provide new knowledge on how raw plant proteins can be valorised for the production of new biomaterials. This may offer extraordinary opportunities towards the design and production of new tailorable biosorbents which can also be exploited for several cycles of purification with minimal reduction in performance. SYNOPSIS: Innovative, sustainable plant-protein biomaterials with tunable properties are presented as green solution for water purification from lead(II) and the structure-function relationship is discussed.

Lead(II) ions adsorption onto amyloid particulates: An in depth study.

The production of new cost-effective biocompatible sorbent sustainable materials, with natural origins, able to remove heavy metals from water resources is nowadays highly desirable in order to reduce pollution and increase clean water availability. In this context, self-assembled protein materials with amyloid structures seem to have a great potential as natural platform for a broader development of highly-tunable structures. In this work we show how protein particulates, a generic form of protein aggregates, with spherical micro sized shape can be used as adsorbents of Pb2+ ions from aqueous solution. The effect of pH, ionic medium, ionic strength and temperature of the metal ion solution on the adsorption ability and affinity has been evaluated revealing the complexity of adsorption mechanisms which are the result of the balance of specific interactions with functional groups in protein structure and not specific ones common to all polypeptide chains, and possibly related to amyloid state and to modification of particulates hydration layer.