Preparation of robust biocatalyst based on cross-linked enzyme aggregates entrapped in three-dimensionally ordered macroporous silica.
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.
School of Chemical Engineering and Technology, Hebei University of Technology , 8 Guangrong Road, Hongqiao District, Tianjin China.
Yanjun
Y
Jiang
Lianlian
L
Shi
Yan
Y
Huang
Jing
J
Gao
Xu
X
Zhang
Liya
L
Zhou
D000645:Ammonium Sulfate / Q000737:chemistry; D055162:Biocatalysis; D002175:Candida / Q000201:enzymology; D004795:Enzyme Stability; D005976:Glutaral / Q000737:chemistry; D008049:Lipase / Q000737:chemistry*; D008855:Microscopy, Electron, Scanning; D012822:Silicon Dioxide / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
D012822:Silicon Dioxide; D008049:Lipase; D000645:Ammonium Sulfate; D005976:Glutaral