Fonseca L P, Cardoso J P, Cabral J M
Laboratorio de Engenharia Bioquimica, Instituto Superior Técnico, Lisboa, Portugal.
J Chem Technol Biotechnol. 1993;58(1):27-37. doi: 10.1002/jctb.280580105.
Penicillin acylase (EC 3.5.1.11) was immobilized by covalent binding on a silica gel carrier activated by silanization. High immobilization yields, operational stability, enzyme loading and support reutilization capacity were obtained. The effects of several variables on the activation of the support and on the immobilization method were studied. Other supports and immobilization methods were assessed for the immobilization of penicillin acylase and compared with the basic process used. Activity versus temperature, pH, buffer molarity and penicillin concentration profiles were determined and compared for the free, crosslinked and covalently-bound silica carrier penicillin acylase preparations. The hydrolysis performance of the latter preparation was assessed in a batch basket reactor and the time course of the hydrolysis reaction modelled by a two parameter model equation. The operational stabilities of penicillin acylase coupled covalently to the silica gel support and immobilized by a crosslinking procedure using glutaraldehyde were also compared.
青霉素酰化酶(EC 3.5.1.11)通过共价结合固定在经硅烷化活化的硅胶载体上。获得了高固定化产率、操作稳定性、酶负载量和载体重复利用能力。研究了几个变量对载体活化和固定化方法的影响。评估了其他载体和固定化方法用于青霉素酰化酶的固定,并与所使用的基本方法进行比较。测定并比较了游离的、交联的和共价结合硅胶载体的青霉素酰化酶制剂的活性与温度、pH、缓冲液摩尔浓度和青霉素浓度的关系曲线。在间歇式篮式反应器中评估了后一种制剂的水解性能,并通过双参数模型方程对水解反应的时间进程进行建模。还比较了通过共价偶联到硅胶载体上以及使用戊二醛通过交联程序固定的青霉素酰化酶的操作稳定性。