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• W2003233519 abstract "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." @default.
• W2003233519 created "2016-06-24" @default.
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• W2003233519 date "2010-10-01" @default.
• W2003233519 modified "2023-09-26" @default.
• W2003233519 title "Covalent immobilization of penicillin G acylase on aminopropyl-functionalized mesostructured cellular foams" @default.
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• W2003233519 doi "https://doi.org/10.1016/j.biortech.2010.04.067" @default.
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