Gallium-binding peptides as a tool for the sustainable treatment of industrial waste streams

JOURNAL OF HAZARDOUS MATERIALS

卷:414

Article

Schoenberger, Nora^1,2  Taylor, Corey³  Schrader, Martin²  Drobot, Bjoern³  Matys, Sabine²  Lederer, Franziska L.²  Pollmann, Katrin² 

[1] TU Bergakad Freiberg, Inst Nonferrous Met & Purest Mat, Leipziger Str 32, D-09599 Freiberg, Germany

[2] Helmholtz Zentrum Dresden Rossendorf, Helmholtz Inst Freiberg Resource Technol, Bautzner Landstr 400, D-01328 Dresden, Germany

[3] Helmholtz Zentrum Dresden Rossendorf, Inst Resource Ecol, Bautzner Landstr 400, D-01328 Dresden, Germany

关键词: Industrial wastewater;    Peptide-based material;    Biosorption;    Gallium;    Arsenic;    Computer modeling;    Isothermal titration microcalorimetry;   

DOI  :  10.1016/j.jhazmat.2021.125366

来源: Elsevier

【 摘 要 】

Here we provide a proof of principle for an application-oriented concept for the peptide-based recovery of gallium in industrial wastewater, which was supported by biosorption studies with a real wastewater sample. We investigated the interaction of the gallium-binding peptides TMHHAAIAHPPH, NYLPHQSSSPSR, SQALSTSRQDLR, HTQHIQSDDHLA, and NDLQRHRLTAGP with gallium and arsenic through different experimental and computational approaches. Data obtained from isothermal titration microcalorimetry indicated a competitive influence by the presence of acetate ions with an exothermic contribution to the otherwise endothermic peptide gallium interactions. For peptide HTQHIQSDDHLA, a stabilizing influence of acetate ions on the metal peptide interaction was found. Peptide NYLPHQSSSPSR showed the highest affinity for gallium in ITC studies. Computational modeling of peptide NYLPHQSSSPSR was used to determine interaction parameters and to explain a possible binding mechanism. Furthermore, the peptides were immobilized on polystyrene beads. Thus, we created a novel and exceptionally robust peptide-based material for the biosorption of gallium from an aqueous solution. Data obtained from isothermal titration microcalorimetry indicated a competitive influence by the presence of acetate ions with an exothermic contribution to the otherwise endothermic peptide gallium interactions. For peptide HTQHIQSDDHLA, a stabilizing influence of acetate ions on the metal peptide interaction was found. Peptide NYLPHQSSSPSR showed the highest affinity for gallium in ITC studies. Computational modeling of peptide NYLPHQSSSPSR was used to determine interaction parameters and to explain a possible binding mechanism. Furthermore, the peptides were immobilized on polystyrene beads. Thus, we created a novel and exceptionally robust peptide-based material for the biosorption of gallium from an aqueous solution.

【 授权许可】

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