Construction of supramolecular laccase enzymes and understanding of catalytic dye degradation using multispectral and molecular docking approaches
Literature Information
Qingteng Zhou, Kaijie Ni, Francesca M. Kerton
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.
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Source Journal
Reaction Chemistry & Engineering

Reaction Chemistry & Engineering is an interdisciplinary journal reporting cutting-edge research focused on enhancing the understanding and efficiency of reactions. Reaction engineering leverages the interface where fundamental molecular chemistry meets chemical engineering and technology. Challenges in chemistry can be overcome by the application of new technologies, while engineers may find improved solutions for process development from the latest developments in reaction chemistry. Reaction Chemistry & Engineering is a unique forum for researchers whose interests span the broad areas of chemical engineering and chemical sciences to come together in solving problems of importance to wider society. All papers should be written to be approachable by readers across the engineering and chemical sciences. Papers that consider multiple scales, from the laboratory up to and including plant scale, are particularly encouraged.










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