不同介孔材料固定青霉素酰化酶的稳定性研究  

Stability of Penicillin G Acylase Immobilized on Different Silica Mesoporous Materials

作　　者：高波[1,2] 朱广山[1] 付学奇[2] 辛明红[1] 陈静[1] 王春雷[1] 裘式纶[1] 

机构地区：[1]吉林大学化学学院,无机合成与制备化学国家重点实验室,吉林大学生命科学学院长春130012 [2]吉林大学生命科学学院,长春130012

出　　处：《高等学校化学学报》2005年第10期1852-1854,共3页Chemical Journal of Chinese Universities

基　　金：国家自然科学基金(批准号:29873017;20101004);国家重大基础研究"九七三"计划(批准号:G2000077507)资助.

摘　　要：Silica mesoporous materials were synthesized and used as the supporting materials for immobilization of enzyme.Penicillin G acylase,an enzyme which was used to produce 6-APA in pharmaceutical industry,was immobilized in the mesoporous materials by the immersion method.The stabilities of the immobilized penicillin G acylase were studied.After incubation at 60 ℃ for 2 h,the activity of immobilized penicillin G acylase remained 80% in the best case.At higher or lower pH,the free enzyme was deactivated quickly,while the immobilized enzyme still retained active.The result of operational stability showed that the immobilized(enzyme) retained 70% of its initial activity after operating for 6 times.These results showed that the stabilities of immobilized penicillin G acylase,related to the pore size of mesoporous materials,were increased significantly compared with those of free enzyme.The improvement of stabilities of immobilized enzyme was significant when the pore size of the mesoporous materials matched the enzyme molecule size.Silica mesoporous materials were synthesized and used as the supporting materials for immobilization of enzyme. Penicillin G acylase, an enzyme which was used to produce 6-APA in pharmaceutical industry, was immobilized in the mesoporous materials by the immersion method. The stabilities of the immobilized penicillin G acylase were studied. After incubation at 60 ℃ for 2 h, the activity of immobilized penicillin G acylase remained 80% in the best case. At higher or lower pH, the free enzyme was deactivated quickly, while the immobilized enzyme still retained active. The result of operational stability showed that the immobilized enzyme retained 70% of its initial activity after operating for 6 times. These results showed that the stabilities of immobilized penicillin G acylase, related to the pore size of mesoporous materials, were increased significantly compared with those of free enzyme. The improvement of stabilities of immobilized enzyme was significant when the pore size of the mesoporous materials matched the enzyme molecule size.

关 键 词：介孔材料 固定化酶 青霉素酰化酶 稳定性 

分 类 号：O629[理学—有机化学]