摘要
制备了含钴MCM-48和MCM-41的介孔分子筛,用作酶生物催化剂固定化的载体.采用XRD、低温N2吸附及FT-IR等方法研究了介孔载体的结构特征、表面酸性和对青霉素酰化酶(Penicillin G Acylase,PGA)的固定化作用.结果表明,Co-MCM-48与Co-MCM-41介孔分子筛表面存在着弱酸性高浓度的自由羟基,为酶的固定化提供了功能性基团和适宜的微环境.固定化酶PGA/Co-MCM-48水解青霉素G的表观活性为1 682 IU/g,约是PGA/Co-MCM-41水解青霉素G表观活性的2.4倍.经6次连续操作使用,PGA/Co-MCM-48的水解活性降至1 375 IU/g,保持其初始活性的81%,而PGA/Co-MCM-41保持其初始活性的42%.Co-MCM-48固定化青霉素酰化酶的活性和操作稳定性显著好于Co-MCM-41固定化酶.
The mesoporous MCM-48 and MCM-41 containing cobalt in the frameworks were synthesized and used as the support for the immobilization of the enzyme biocatalyst. The structural characteristics, surface properties and immobilization for penicillin G acylase （PGA） of the mesoporous supports were investigated by XRD, N2-adsorption and FT-IR spectrum. The results show that there is a high concentration of the weakly acidic hydroxyl groups on the surface of Co-MCM-48 and Co-MCM-41 mesoporous molecular sieves acting as the functional groups coupling the enzyme molecules and offer the suitable microenvironment for the immobilization of penicillin G acylase. For the hydrolysis of penicillin G potassium by PGA/MCM-48, the apparent activity of 1682 IU/g was obtained, which is about 2.4 times more than that by PGA/MCM-41. The apparent activity of PGA/MCM-48 decreased to 1 375 IU/g and remained about 81% its initial activity after used consecutive hydrolysis of penicillin G for 6 times. The PGA/MCM-41 kept 42% its initial activity after the same operations. K
出处
《宁夏大学学报（自然科学版）》
CAS
北大核心
2006年第3期243-247,共5页
Journal of Ningxia University(Natural Science Edition)
基金
国家重大基础研究前期研究专项基金资助项目(2004CCA05900)
宁夏高校科研基金资助项目(NU00405)
