文献类型：期刊文献

英文题名：Novel support of MCM-48 molecular sieve for immobilization of penicillin G acylase

作者：Xue, P; Lu, GZ; Guo, YL; Wang, YS; Guo, Y

机构：[1]E China Univ Sci & Technol, Res Inst Ind Catalysis, Shanghai 200237, Peoples R China;[2]Ningxia Univ, Key Lab Energy Sources & Chem Engn, Yinchuan 750021, Peoples R China

年份：2004

卷号：30

期号：2

起止页码：75

外文期刊名：JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000222111700004)】；

语种：英文

外文关键词：MCM-48; Co-MCM-48; penicillin G acylase; immobilization; hydrolysis

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, N-2 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 1682 U/g. After used for six cycles, PGA/MCM-48(0.01) can keep 1375 U/g of the specific activity. If MCM-41 was used as the support, the activity of immobilized PGA is only 402 U/g. (C) 2004 Elsevier B.V. All rights reserved.