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不同介孔材料固定青霉素酰化酶的稳定性研究 被引量:21

Stability of Penicillin G Acylase Immobilized on Different Silica Mesoporous Materials
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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.
出处 《高等学校化学学报》 SCIE EI CAS CSCD 北大核心 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.
关键词 介孔材料 固定化酶 青霉素酰化酶 稳定性 Silica mesoporous materials Immobilized enzyme Penicillin G acylase Stability
作者简介 联系人简介:裘式纶(1948年出生),男,博士,教授,博士生导师,主要从事无机化学研究.E-mail:sqiu@mail.jlu.edu.cn
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