Construction of supramolecular laccase enzymes and understanding of catalytic dye degradation using multispectral and molecular docking approaches?

Reaction Chemistry & Engineering Pub Date: 2021-07-26 DOI: 10.1039/D1RE00111F

Abstract

A non-covalent supramolecular enzyme system, which is formed by non-covalent interactions of an enzyme with substrate analogs, shows better enzyme catalytic activity than the enzyme itself. A non-covalent supramolecular laccase-dye substrate analog system (SL-DSA) was designed to confirm the enzyme catalyzing mechanism. A range of spectral and electrochemical methods showed that the non-covalent interaction is important in the catalytic degradation reaction of 13 dyes. The decolorization rate was 10–54% higher than with laccase (LAC) alone. Thus, the SL-DSA has better catalytic activity than LAC itself in the three-step degradation reaction of dyes. The enzymatic mechanism of SL-DSA identified may act to supplement the mechanism of the enzyme binding directly with the substrate.

Graphical abstract: Construction of supramolecular laccase enzymes and understanding of catalytic dye degradation using multispectral and molecular docking approaches
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