Preparation of Robust Biocatalyst Based on Cross-Linked Enzyme Aggregates Entrapped in Three-Dimensionally Ordered Macroporous Silica
Preparation of Robust Biocatalyst Based on Cross-Linked Enzyme Aggregates Entrapped in Three-Dimensionally Ordered Macroporous Silica
复制标题
基于三维有序大孔二氧化硅中交联酶聚集体的鲁棒生物催化剂的制备
DOI：
10.1021/am405104b
复制
发表时间：
2014-02-26
影响因子：
9.5
通讯作者：
Zhou, Liya
中科院分区：
文献类型：
--
作者：
Jiang, Yanjun;Shi, Lianlian;Zhou, Liya
为了提供高度稳定和活性的生物催化剂，脂肪酶念珠菌交联酶聚集体（CLEA）。 99-125是在三维有序大孔二氧化硅材料(CLEAs-LP@3DOM-SiO2)中制备的。脂肪酶念珠菌 sp. 99-125首先在3DOM SiO2的孔中沉淀（命名为EAs-LP@3DOM-SiO2），并进一步通过戊二醛交联形成CLEAs-LP@3DOM-SiO2。使用饱和硫酸铵作为沉淀剂，使用浓度为0.25%（w/w）的戊二醛作为交联剂。与EAs-LP@3DOM-SiO2和天然脂肪酶相比，CLEAs-LP@3DOM-SiO2表现出优异的热稳定性和机械稳定性，在有机相和水相中振荡16天后仍能保持85%以上的初始活性。当CLEAs-LP@3DOM-SiO2应用于酯化和酯交换反应时，提高了活性和可重复使用性。该方法可用于固定其他感兴趣的酶。
With the aim to provide a highly stable and active biocatalyst, cross-linked enzyme aggregates (CLEAs) of lipase Candida sp. 99-125 were prepared in three-dimensionally ordered macroporous silica materials (CLEAs-LP@ 3DOM-SiO2). Lipase Candida sp. 99-125 was first precipitated in the pores of 3DOM SiO2 (named EAs-LP@3DOM-SiO2), and further cross-linked by glutaraldehyde to form CLEAs-LP@3DOM-SiO2. Saturated ammonium sulfate was used as a precipitant and glutaraldehyde with a concentration of 0.25% (w/w) was employed as a cross-linker. Compared with EAs-LP@ 3DOM-SiO2 and native lipase, CLEAs-LP@3DOM-SiO2 exhibited excellent thermal and mechanical stability, and could maintain more than 85% of initial activity after 16 days of shaking in organic and aqueous phase. When CLEAs-LP@3DOM-SiO2 was applied in esterification and transesterification reactions, improved activity and reusability were achieved. This method can be used for the immobilization of other enzymes of interest.