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Abstract
Chiral carbon dots (CDots) have received much attention in biocatalysis due to their biocompatibility and low toxicity. For chiral CDots-enzyme hybrid system, great efforts are needed to understand the interactions between chiral CDots and enzymes. Here, chiral CDots (L-/D-Trp-CDots) from citric acid and L-/D-tryptophan were designed and synthesized. The obtained L-Trp-CDots were used to regulate the activity of laccase, showing an 87.26 % inhibition rate of laccase, which is significantly higher than that of D-Trp-CDots (57.84 %) under the same reaction conditions. It is chiral functional groups rather than the carbon core play the important role in chiral CDots for regulating enzymatic activity in this system.
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