Please use this identifier to cite or link to this item:
|Title:||Design of large-pore mesoporous materials for immobilization of penicillin G acylase biocatalyst|
Functionalization of mesoporous silicas
Penicillin G acylase
|Citation:||Chong, A.S.M., Zhao, X.S. (2004-09-01). Design of large-pore mesoporous materials for immobilization of penicillin G acylase biocatalyst. Catalysis Today 93-95 : 293-299. ScholarBank@NUS Repository. https://doi.org/10.1016/j.cattod.2004.06.064|
|Abstract:||In this study, functionalization of large-pore nanoporous silica materials was carried out by condensation of tetraethylorthosilicate (TEOS) and 3-aminopropyltriethoxysilane (APTES), 3-mercaptopropyltrimethoxysilane (MPTMS), phenyltrimethoxysilane (PTMS), vinyltriethoxysilane (VTES), and 4-(triethoxysilyl)butyronitrile (TSBN), respectively, in the presence of non-ionic surfactant under acidic conditions. The TSBN functionality was subsequently converted to carboxyl group while APTES was further functionalized with glutardialdehyde, a cross linker. The various functionalized materials were used as supports for immobilization of enzyme penicillin G acylase (PGA). Experimental data showed that the functionalized materials except for the material functionalized with MPTMS possess a faster loading kinetics and a higher loading amount of enzyme PGA than the pure-silica counterpart. The enzymatic catalytic activities of the immobilized biocatalysts varied from 52.2 to 167.5U/g of solid. The glutardialdehyde-activated material displayed the highest initial immobilized enzyme activity and the most stable activity among all the support materials. PGA immobilized on VTES-functionalized nanoporous silica showed the highest initial enzymatic activity (67.7U/mg of PGA, much higher than that of free PGA (300U/mg of PGA). Experimental data along with theoretical analysis results indicate that glutardialdehyde is a good cross linker, offering covalent binding of PGA with the support materials while VTES-functionalized nanoporous silica is a very good potential support for physical entrapment of PGA enzyme. © 2004 Elsevier B.V. All rights reserved.|
|Source Title:||Catalysis Today|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on May 20, 2018
WEB OF SCIENCETM
checked on Apr 10, 2018
checked on May 11, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.