Biomimetic Mineralization of Cytochrome c Improves the Catalytic Efficiency and Confers a Functional Multi-Enzyme Composite
文献类型： 外文期刊
作者： Gong, Xiao-Qing 1 ; Wei, Chuan-Wan 1 ; Xu, Jia-Kun 2 ; Wang, Xiao-Juan 1 ; Gao, Shu-Qin 4 ; Lin, Ying-Wu 1 ;
作者机构： 1.Univ South China, Sch Chem & Chem Engn, Hengyang 421001, Peoples R China
2.Chinese Acad Fishery Sci, Key Lab Sustainable Dev Polar Fisheries, Yellow Sea Fisheries Res Inst, Qingdao, Shandong, Peoples R China
3.Pilot Natl Lab Marine Sci & Technol, Lab Marine Drugs & Byprod, Qingdao 266071, Shandong, Peoples R China
4.Univ South China, Lab Prot Struct & Funct, Hengyang 421001, Peoples R China
5.Univ South China, Hunan Key Lab Design & Applicat Actinide Complexe, Hengyang 421001, Peoples R China
关键词： enzymatic immobilization; biomimetic mineralization; multi-enzyme; bioinorganic hybrid material; biosensors
期刊名称：CATALYSTS （ 影响因子：4.146； 五年影响因子：4.399 ）
ISSN：
年卷期： 2019 年 9 卷 8 期
页码：
收录情况： SCI
摘要： The encapsulated enzyme system by metal-organic frameworks (MOFs) exhibits great potential in biofuel cells, pharmaceuticals, and biocatalysis. However, the catalytic efficiency and the enzymatic activity are severely hampered due to enzyme leaching and deficiency of storage stability. In this study, we immobilized cytochrome c (Cyt c) into dimethylimidazole-copper (Cu(Im)(2)) by biomimetic mineralization, and constructed a bioinorganic hybrid material, termed Cyt c@Cu(Im)(2). Encapsulated Cyt c in Cu(Im)(2) with a nanosheet structure exhibited significantly improved catalytic efficiency, enzymatic activity and kinetic performance. The catalytic efficiency (k(cat)/K-m) for Cyt c@Cu(Im)(2) was similar to 20-fold higher compared to that of free Cyt c. Moreover, the increased activity was not affected by long-term storage. Based on this system, we further constructed a multi-enzyme composite with glucose-oxidase (GOx), termed GOx-Cyt c@Cu(Im)(2), which exhibited greatly improved enzymatic activity, stability, and excellent selectivity for the detection of low concentrations of glucose. This strategy may provide new insights into the design of enzymes with high activity and stability, as well as the construction of multi-enzyme systems.
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