Preparation and activity exploration of Cu-based laccase mimetic enzyme Cu-MP
The catalytic activity and stability of natural laccase are easily affected by environmental factors.Inspired by the natural laccase active center and electron transfer,a novel laccase mimetic enzyme(Cu-MP)was synthesized by the coordination reaction of 6-mercaptopurine with copper ions.By SEM-EDS,BET,FTIR,XRD and XPS characterization analysis,the results show that Cu-MP has a coral-like porous network structure,thus providing larger specific surface area for catalytic reaction.Cu-MP was synthesized by the coordination of sulfur and base nitrogen(N7)with copper ions.According to the catalytic mechanism,the simulated enzyme Cu-MP acquires electrons from the substrate through copper ions,and then realizes electron transfer according to S—C6—C5—N7 channel.Compared with natural laccase at the same mass concentration,Cu-MP has better affinity for substrate,and vmax is 4.7 times of that of natural laccase.After being stored at room temperature for 7 d,the enzyme activity retention rate reaches 84.03％.After nine cycles of recycling,the enzyme activity retention rate is more than 70％.Even in high salt or organic solution,Cu-MP can still maintain relatively stable catalytic activity.Therefore,Cu-MP can replace natural laccase,especially in some extreme conditions,to treat phenols and other environmental pollutants,is a kind of environmental catalyst with development and application prospects.
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