Supramolecular assembly of benzophenone alanine and copper presents high laccase-like activity for the degradation of phenolic pollutants

Laccases are multicopper oxidases of significant importance for the degradation of phenolic pollutants. Because of the inherent defects of natural laccases in practical applications, herein, we discovered highly effective and non-cytotoxic laccase-like metallo-nanofibers based on the supramolecular assembly of single unnatural amino acid, benzophenone–alanine (BpA), in combination with copper ions. Structural analysis revealed that the catalytic BpA–Cu nanofibers possess a Cu(I)–Cu(II) electron transfer system similar to that in natural laccase. Our BpA–Cu nanofibers exhibit 4 times higher substrate affinity and 24% higher catalytic efficiency than the well-known high-performance industrialized laccase (Novozym 51003) in 2,4-dichlorophenol degradation. In addition, the BpA–Cu nanofibers were demonstrated to be stable (>75% residual activity) in long-term storage at a wide range of pH, ionic strength, temperature, ethanol, and water sample, and to be readily recovered for pollutant degradation, keeping 83% of the laccase activity after 10 catalytic recycles. Remarkably, the nanofibers displayed a wide substrate spectrum, detecting and degrading a variety of phenolic pollutants with high activity than other laccase mimics reported in the literature. Furthermore, the biocompatibility of the material was proved with cultured cells. These findings demonstrated the potential of BpA–Cu nanofibers in mimicking laccases for environmental remediation.