ABSTRACT
As a good alternative for natural enzyme, enzyme mimics with artificial functional materials have attracted considerable attention. However, it remains a great challenge to develop a facile method to design laccase mimic with high catalytic activity, long-term stability and reusability. In this report, we propose the one-pot synthesis of reusable paper filter templated Cu-doped polydopamine membranes (PF@PDA/Cu) with laccase-like activity. Compared with the natural laccase, the PF@PDA/Cu membrane exhibits enhanced catalytic activity for the chemical conversion of hydroquinone into benzoquinone. Interestingly, these membranes present good tolerance to high temperature and the catalytic activity increases with the increase of temperature. Moreover, these membranes could be stored for 7 days and recycled for 5 times with negligible loss of catalytic activity. This work provides a promising paradigm for rational design and practical applications of metal-loading PDA materials based on one-pot synthesis methodology.
Subject(s)
Hydroquinones , Laccase , Benzoquinones , Indoles , PolymersABSTRACT
The development of high-efficiency enzyme mimics is of great significance in the field of biocatalysis. However, it remains challenging to design novel enzyme mimics with multiple enzyme-like activities, excellent stability, and good reusability. Herein, a facile molecular assembly strategy to construct dialdehyde cellulose (DAC) templated Cu-doped polydopamine (DAC@PDA/Cu) membrane with dual enzyme-like activities is presented. The Schiff base bonds formed between polydopamine (PDA) and DAC can not only accelerate the adhesion of PDA thin layer but also contribute to Cu-loading and high stability of DAC@PDA/Cu membrane. Importantly, the assembled DAC@PDA/Cu membrane exhibits a remarkable catalytic activity that is superior to the natural laccase along with high stability and excellent reusability. Moreover, the DAC@PDA/Cu membrane also demonstrates peroxidase-like activity, and it is successfully applied in the sensitive detection of ascorbic acid (AA). This work will provide a new paradigm methodology for rational design and practical applications of enzyme mimics based on bioinspired molecular assemblies.