Covalent immobilization of penicillin G acylase on aminopropyl-functionalized mesostructured cellular foams.
Covalent immobilization of penicillin G acylase on aminopropyl-functionalized mesostructured cellular foams.
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DOI：
10.1016/j.biortech.2010.04.067
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发表时间：
2010-10
影响因子：
11.4
通讯作者：
Junqi Zhao;Yujun Wang;G. Luo;Shenlin Zhu
中科院分区：
文献类型：
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作者：
Junqi Zhao;Yujun Wang;G. Luo;Shenlin Zhu
介孔泡沫材料具有较大的孔径和孔容，适合于生物分子的固定。采用席夫碱法将青霉素酰化酶（PGA）固定在氨丙基化的MCFs上。结果表明，PGA可以通过共价固定在氨丙基功能化的MCFs支持比通过吸附固定在空白MCFs更牢固。经氨丙基化修饰后，PGA的负载量可达443 mg/g（干载体），表观活性可达4138 U/g（干载体）。研究了接枝氨丙基的量对固定化酶活性的影响，发现MCFs与APTS的最佳摩尔比为15：1，固定化PGA的最佳酶分布密度为0.7mg酶/m2 MCFs比表面积。
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 443mg/g (dry support), and the apparent activity could achieve up to 4138U/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 0.7mg enzyme per m2of specific area of MCFs.