Abstract
Supramolecular structures were produced by auto-assembling CuCN blocks derived from copper-lipopeptides (CuLps) isolated from bioleaching liquor. Lipopeptides produced by B. subtilis Hyhel1 have been previously related as responsible by bioleaching and intracellular copper crystal production. However, there were no records relating CuLps to extracellular copper crystal production. To study this process, CuLps were isolated from bioleaching liquor and kept at 8 °C to facilitate the CuLps aggregation. After three months, blue spheres (BS) were observed in the CuLp fraction. These spheres were then analyzed by SEM-EDS, MALDI-TOF-MS/MS, GC-MS and FTIR. SEM-EDS analysis showed that they were formed by polycrystalline structures mainly composed by Cu (46.5% m/m) and positioned concentrically. MALDI-TOF-MS/MS and GCMS showed that peptide bonds of CuLp were broken, producing lipid chains and amino acids free. The FTIR of BS showed three nitro groups: CN, NN and NO, which were not found in the control. These data suggest that the CuLp amino acid produced a CN group linked to copper, as CuCN blocks, that auto-assembled in supramolecular structures. This phenomenon could be explored as a method to recover copper and to obtain supramolecular CuCN structures, which in turn may be used as template for superconductor or computing devices.
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