铜基漆酶模拟酶Cu-MP的制备及活性研究  

Preparation and activity exploration of Cu-based laccase mimetic enzyme Cu-MP

作　　者：孙艺格 徐晨 曹红[2,3] 高云玲 李成[3] 郑兰兰 SUN Yige;XU Chen;CAO Hong;GAO Yunling;LI Cheng;ZHENG Lanlan(College of Chemical Engineering,Zhejiang University of Technology,Hangzhou 310014,China;College of Biological Chemical Sciences and Engineering,Jiaxing University,Jiaxing 314001,China;G60 STI Valley Industry&Innovation Institute,Jiaxing University,Jiaxing 314001,China)

机构地区：[1]浙江工业大学化学工程学院,杭州310014 [2]嘉兴学院生物与化学工程学院,嘉兴314001 [3]嘉兴学院G60科创走廊产业与创新研究院,嘉兴314001

出　　处：《中国有色金属学报》2024年第1期314-328,共15页The Chinese Journal of Nonferrous Metals

基　　金：国家自然科学基金资助项目(21266029);浙江省自然科学基金资助项目(LY17B060011)。

摘　　要：天然漆酶的催化活性和稳定性易受外界环境因素的不良影响,受天然漆酶活性中心和电子转移的启发,利用6-巯基嘌呤与铜离子的配位反应合成一种新型漆酶模拟酶(Cu-MP),并采用SEM-EDS、BET、FTIR、XRD、XPS对其性能进行表征并分析。结果表明:Cu-MP呈珊瑚状多孔网状结构,可为催化反应提供较大的比表面积;6-MP主要通过硫和碱基氮(N7)与铜离子配位合成Cu-MP。催化机理推测,模拟酶Cu-MP通过铜离子从底物获取电子后,按照S-C_(6)-C_(5)-N_(7)通道实现电子转移;与相同质量浓度下的天然漆酶相比,Cu-MP对底物的亲和力更佳,其最大反应速度v_(max)是天然漆酶的4.7倍;在25℃下储存7 d后,Cu-MP的酶活保留率达84.03%;经过9轮循环利用,酶活保留率在70%以上;甚至在高盐或有机溶液中,Cu-MP仍能保持相对稳定的催化活性。因此,Cu-MP可以取代天然漆酶,尤其在一些极端条件下,用于处理酚类等环境污染物,是一种具有发展和应用前景的环境催化剂。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(N_(7))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—C_(6)—C_(5)—N_(7)channel.Compared with natural laccase at the same mass concentration,Cu-MP has better affinity for substrate,and v_(max) 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.

关 键 词：天然漆酶 铜基漆酶模拟酶 Cu-MP 催化机理 酚类污染物 

分 类 号：O641[理学—物理化学]