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<p>Efficient recovery of rare earth elements (REEs) is essential for sustainable technologies. We evaluated a synthetic cyclizable peptide (peptide 2) for bacterial biosorption. Fluorescence resonance energy transfer analysis, utilizing non-linear regression models, revealed that peptide 2 possesses high affinity for middle-range lanthanides, such as Tb<sup>3+</sup>, Gd<sup>3+</sup>, and Dy<sup>3+</sup>. Disulfide-mediated cyclization significantly enhanced binding affinity, yielding a dissociation constant of 2.6&#xa0;nM for Tb<sup>3+</sup>. To develop a practical biosorbent, we engineered <i>Escherichia coli</i> to display peptide 2 on its outer membrane via the OmpC protein. These recombinant strains exhibited a standardized adsorption capacity of up to 1.11&#xa0;mg&#xa0;Tb/g dry biomass, representing a statistically significant improvement of up to 33% compared to the native OmpC control. These results highlight the potential of surface-displayed cyclizable peptides for developing efficient, REE-specific biosorbents.</p>

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Biosorption of rare earth elements by Escherichia coli displaying a cyclizable terbium(III)-binding peptide

  • 期刊论文

  • 发表日期：

    2026年7月23日

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  • Fumika Kojima,
  • Masato Hoshino,
  • Miho Yoshimura,
  • Kaneyoshi Yamamoto

摘要

Efficient recovery of rare earth elements (REEs) is essential for sustainable technologies. We evaluated a synthetic cyclizable peptide (peptide 2) for bacterial biosorption. Fluorescence resonance energy transfer analysis, utilizing non-linear regression models, revealed that peptide 2 possesses high affinity for middle-range lanthanides, such as Tb3+, Gd3+, and Dy3+. Disulfide-mediated cyclization significantly enhanced binding affinity, yielding a dissociation constant of 2.6 nM for Tb3+. To develop a practical biosorbent, we engineered Escherichia coli to display peptide 2 on its outer membrane via the OmpC protein. These recombinant strains exhibited a standardized adsorption capacity of up to 1.11 mg Tb/g dry biomass, representing a statistically significant improvement of up to 33% compared to the native OmpC control. These results highlight the potential of surface-displayed cyclizable peptides for developing efficient, REE-specific biosorbents.