A novel support of MCM-48 molecular sieve for immobilization of penicillin G acylase

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• 作者：Xue ; Ping ; Lu ; Guanzhong ; Guo ; Yanglong ; Wang ; Yunsong ; Guo ; Yun
• 关键词：MCM-48 ; Co-MCM-48 ; Penicillin G acylase ; Immobilization ; Hydrolysis
• 刊名：Journal of Molecular Catalysis B ; Enzymatic
• 出版年：2004
• 期刊代码：55_13811177
• 类别：ce
• 出版时间：August 3, 2004
• 卷：30
• 期：2
• 页码：75-81
• 文件大小：186 K

摘要

As a novel support of immobilizing penicillin G acylase (PGA), MCM-48 and Co-MCM-48 molecular sieves were synthesized and characterized by XRD, N₂ adsorption, NH₃-TPD, FT-IR and so on. The studies show that MCM-48 and Co-MCM-48 has well ordered long-range structure, narrow pore size distribution, larger surface area and higher concentration of the weakly acidic silanol groups on their surface. Penicillin G acylase was immobilized on MCM-48 or Co-MCM-48 by interacting silanol groups on the surface. The presence of cobalt in the framework of MCM-48 increases the amount of the weak acid sites. For the hydrolysis of penicillin G catalyzed by PGA/Co-MCM-48 (Co/Si=0.01), its specific activity reaches 1682U/g. After used for six cycles, PGA/MCM-48(0.01) can keep 1375U/g of the specific activity. If MCM-41 was used as the support, the activity of immobilized PGA is only 402U/g.