Covalent immobilization of penicillin G acylase on aminopropyl-functionalized mesostructured cellular foams.
Mesostructured cellular foams (MCFs) are suitable for biomolecular immobilization because of their relatively large-pore diameter and pore volume. Penicillin G acylase (PGA) was immobilized on aminopropyl-functionalized MCFs through Schiff base reaction. It is shown that PGA could be fixed more firmly through the covalent immobilization on aminopropyl-functionalized MCFs support than through the adsorption immobilization on blank MCFs. The PGA loading amount on the aminopropyl-functionalized MCFs could reach 443 mg/g (dry support), and the apparent activity could achieve up to 4138 U/g (dry support). The influence of the amount of grafted aminopropyl group was studied, and it is found that the optimal molar ratio of MCFs to APTS was 15/1; in addition, the suitable enzyme distribution density for the specific activity of the immobilized PGA was 0.7 mg enzyme per m(2) of specific area of MCFs.
Zhao
Junqi
J
The State Key Laboratory of Chemical Engineering, Department of Chemical Engineering, Tsinghua University, Beijing, China.
Wang
Yujun
Y
Luo
Guangsheng
G
Zhu
Shenlin
S
D000327:Adsorption; D000588:Amines / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D009584:Nitrogen / Q000737:chemistry; D010399:Penicillin Amidase / Q000378:metabolism*; D016062:Porosity; D012822:Silicon Dioxide / Q000737:chemistry*; D013696:Temperature
D000588:Amines; D004800:Enzymes, Immobilized; D012822:Silicon Dioxide; D010399:Penicillin Amidase; D009584:Nitrogen