Self-Assembly of Amphiphilic Janus Particles into Monolayer Capsules for Enhanced Enzyme Catalysis in Organic Media

被引:88
作者
Cao, Wei [1 ]
Huang, Renliang [2 ]
Qi, Wei [1 ,3 ]
Su, Rongxin [1 ,3 ]
He, Zhimin [1 ]
机构
[1] Tianjin Univ, Sch Chem Engn & Technol, State Key Lab Chem Engn, Tianjin 300072, Peoples R China
[2] Tianjin Univ, Sch Environm Sci & Engn, Tianjin 300072, Peoples R China
[3] Collaborat Innovat Ctr Chem Sci & Engn Tianjin, Tianjin 300072, Peoples R China
关键词
Janus particle; capsule; Pickering emulsion; self-assembly; enzyme immobilization; LIQUID-LIQUID INTERFACES; COLLOIDAL PARTICLES; IMMOBILIZATION; COLLOIDOSOMES; WATER; MICROCAPSULES; STABILIZATION; NANOPARTICLES; SURFACTANTS; EMULSIONS;
D O I
10.1021/am5065156
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
Encapsulation of enzymes during the creation of an emulsion is a simple and efficient route for enhancing enzyme catalysis in organic media. Herein, we report a capsule with a shell comprising a monolayer of silica Janus particles (JPs) (referred to as a monolayer capsule) and a Pickering emulsion for the encapsulation of enzyme molecules for catalysis purposes in organic media using amphiphilic silica JPs as building blocks. We demonstrate that the JP capsules had a monolayer shell consisting of closely packed silica JPs (270 nm). The capsules were on average 5-50 μM in diameter. The stability of the JP capsules (Pickering emulsion) was investigated with the use of homogeneous silica nanoparticles as a control. The results show that the emulsion stabilized via amphiphilic silica JPs presented no obvious changes in physical appearance after 15 days, indicating the high stability of the emulsions and JP capsules. Furthermore, the lipase from Candida sp. was chosen as a model enzyme for encapsulation within the JP capsules during their formation. The catalytic performance of lipase was evaluated according to the esterification of 1-hexanol with hexanoic acid. It was found that the specific activity of the encapsulated enzymes (28.7 U mL-1) was more than 5.6 times higher than that of free enzymes in a biphasic system (5.1 U mL-1). The enzyme activity was further increased by varying the volume ratio of water to oil and the JPs loadings. The enzyme-loaded capsule also exhibited high stability during the reaction process and good recyclability. In particular, the jellification of agarose in the JP capsules further enhanced their operating stability. We believe that the monolayer structure of the JP capsules, together with their high stability, rendered the capsules to be ideal enzyme carriers and microreactors for enzyme catalysis in organic media because they created a large interfacial area and had low mass transfer resistance through the monolayer shell. © 2014 American Chemical Society.
引用
收藏
页码:465 / 473
页数:9
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