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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

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【作者】 程仕伟王玉芳步长平张桂春

【Author】 CHENG Shi-wei~1,WANG Yu-fang~2,BU Chang-ping~1,ZHANG Gui-chun~1 (1.School of Life Sciences,Ludong University,Yantai 264025,China;2.School of Information Science and Engineering,Shandong Normal University,Jinan 250014,China)

【机构】 鲁东大学生命科学学院山东师范大学信息科学与工程学院

【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。

【Abstract】 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 Alcaligenes faecalis 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.

  • 【文献出处】 食品与药品 ,Food and Drug , 编辑部邮箱 ,2012年03期
  • 【分类号】Q814.2
  • 【下载频次】106
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