Highly active, stable and self-antimicrobial enzyme catalysts prepared by biomimetic mineralization of copper hydroxysulfateElectronic supplementary information (ESI) available. See DOI: 10.1039/c6nr06115j

• Main Authors: Li, Zhixian, Ding, Yi, Li, Shaomin, Jiang, Yanbin, Liu, Zheng, Ge, Jun
• Format: Journal Article
• Language: English
• Published: 14.10.2016
• ISSN: 2040-3364; 2040-3372
• DOI: 10.1039/c6nr06115j

A nature-inspired approach to encapsulate enzymes in spindle-like copper hydroxysulfate nanocrystals was developed by a biomimetic mineralization process. Several types of enzymes including glucose oxidase (GOx), horseradish peroxidase (HRP), Candida antarctica lipase B (CALB) and cytochrome c (Cyt c) were successfully encapsulated in copper hydroxysulfate nanocrystals quickly (within 1 hour) with maintained or even greatly enhanced catalytic efficiencies ( k cat / K M of Cyt c showed a 143-fold increase) and high stabilities, demonstrating the feasibility of utilizing copper hydroxysulfate nanocrystals as a novel type of nanocarrier for enzyme immobilization. In addition, by this approach, for the first time, we showed that an immobilized enzyme can be endowed with self-antibacterial activity by an inorganic component. This self-antibacterial performance together with the improved catalytic efficiencies and stabilities can greatly benefit the enzymatic catalysis in aqueous media and promote the future development of novel biosensors. To address the activity-stability contradiction, enzymes encapsulated in spindle-like copper hydroxysulfate nanocrystals by a nature-inspired, facile and general approach exhibit both high activity and high stability, and additional self-antimicrobial properties at the same time.