Activity, Recyclability, and Stability of Lipases Immobilized on Oil-Filled Spherical Silica Nanoparticles with Different Silica Shell Structures
Activity, Recyclability, and Stability of Lipases Immobilized on Oil-Filled Spherical Silica Nanoparticles with Different Silica Shell Structures
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DOI：
10.1002/cctc.201300072
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发表时间：
2013-08-01
期刊：
影响因子：
4.5
通讯作者：
Yamashita, Hiromi
中科院分区：
文献类型：
--
作者：
Kuwahara, Yasutaka;Yamanishi, Takato;Yamashita, Hiromi
将南极假丝酵母脂酶ea固定在填充油芯的球形二氧化硅纳米颗粒和不同结构的油致介孔二氧化硅纳米颗粒上。在环境合成条件下，将酶直接加入到水包油乳液体系中实现酶的固定化，并通过在初始合成介质中加入助溶剂乙醇来控制硅壳结构。详细的结构分析表明，在硅壳中形成了具有3.4 ~ 4.2 nm介孔的充油球形二氧化硅纳米颗粒；随着乙醇的加入，这些孔隙的厚度和孔隙特征发生了明显的变化。生物催化过程中酶活性的保持受到二氧化硅壳结构特性的显著影响，并且发现厚而致密的二氧化硅壳是提供活性、可回收和稳定的生物催化剂所必需的。此外，芯腔内的油包封对实现高催化效率起着重要作用。
Candida antarctica lipaseA was immobilized on spherical silica nanoparticles with oil-filled core and oil-induced mesoporous silica shell with different silica shell structures. The immobilization of enzymes was achieved by directly adding enzymes to the oil-in-water emulsion system under ambient synthesis conditions, and the silica shell structure was controlled by the addition of the cosolvent ethanol to the initial synthesis medium. Detailed structural analysis revealed the formation of oil-filled spherical silica nanoparticles with 3.4-4.2 nm mesopores randomly arranged in the silica shell; the thickness and pore characteristics of these pores markedly changed with the addition of ethanol. The retention of the enzyme activity during biocatalysis was significantly affected by the structural properties of the silica shells, and it was found that a thick and dense silica shell is essential to afford an active, recyclable, and stable biocatalyst. Furthermore, the oil encapsulated within the core cavity was found to play an important role in achieving a high catalytic efficiency.