交联青霉素G酰化酶聚集体制备及其催化特性研究  

Preparation of Cross-linked Penicillin G Acylase Aggregates and Its Catalytic Property

作　　者：程仕伟[1] 王玉芳[2] 步长平[1] 张桂春[1] 

机构地区：[1]鲁东大学生命科学学院,山东烟台264025 [2]山东师范大学信息科学与工程学院,山东济南250014

出　　处：《食品与药品》2012年第2期77-81,共5页Food and Drug

摘　　要：目的考察交联青霉素G酰化酶聚集体催化特性,探讨其应用潜力。方法以硫酸铵为沉淀剂获得青霉素G酰化酶蛋白沉淀,戊二醛交联沉淀的蛋白质制备交联酶聚集体,在此基础上研究交联酶聚集体的催化特性。结果交联粪产碱杆菌来源青霉素G酰化酶聚集体的最适反应温度55℃,最适pH 9.0,其酸碱和热稳定性均优于游离酶,重复使用13批次几乎无酶活性丢失,反应20批次后仍有50.9%的活性。结论交联酶聚集体的稳定性较游离酶好,具有一定的工业应用前景。Objective Cross-linked enzyme aggregates （CLEA） have more advantages than carrier-bound immobilized enzymes. And this paper explored the potential application of cross-linked aggregates of penicillin G acylase by investigating its catalytic property. Methods The preparation of cross-linked aggregates about penicillin G acylase from Alcaligenesfaecalis was as follows： the enzyme was precipitated by ammonium sulfate and then was cross-linked with glutaraldehyde. Furthermore, its catalytic property was studied. Results The optimum reaction temperature and pH of the cross-linked penicillin G acylase aggregates were 55 ℃ and pH9.0. In addition, they had better thermal and pH stability than the free enzyme. The activity hardly lost after 13 cycles, and there was even 50.9% of the enzyme activity after 20 cycles. Conclusion The cross-linked penicillin G acylase aggregates have good operation stability and potential application as an industrial biocatalyst.

关 键 词：青霉素G酰化酶 交联酶聚集体 催化特性 固定化酶 

分 类 号：Q814.2[生物学—生物工程]