介孔纳米孔道中单维交联酶策略固定青霉素酰化酶  

One-dimensional cross-linked enzyme aggregate strategy for penicillin acylase immobilization in mesopores

作　　者：姜波[1] 周成[1] 绳则翠[1] 祝社民[2] 沈树宝[1] 

机构地区：[1]南京工业大学生物与制药工程学院,江苏南京210009 [2]南京工业大学材料科学与工程学院,江苏南京210009

出　　处：《化学工程》2010年第12期68-71,75,共5页Chemical Engineering(China)

基　　金："十一五"国家"863"项目(2009AA05Z313;2006AA02Z211);国家自然科学基金资助项目(20376034);江苏省自然科学基金资助项目(BK2006181);江苏省高校研究生创新计划项目(2007);南京工业大学高校博士生创新计划(BSCX200910)

摘　　要：为解决酶固定化过程中稳定性较差的问题,将单维交联酶策略引入青霉素酰化酶的固定化中,通过在介孔泡沫硅载体(MCFs)表面初步吸附作用将酶固定,再用对本醌对酶分子进行交联,从而制得单维交联酶聚体。实验结果显示:单维交联酶聚体(CLEA)的稳定性有明显提高,最适温度从游离酶的45℃上升到55℃,催化温度的适用范围更宽,在50℃下热处理25 h仍保持74.4%活力,在测试操作稳定性方面,连续操作15次,其酶活保持在61.9%。In order to improve the stability of penicillin acylase（PA）,the strategy of one-dimensional cross-linked enzyme aggregate（CLEA） was introduced to the immobilization process of PA.Mesocellular siliceous foams（MCFs） with large pore diameter were synthesized,and PA was coupled to MCFs through adsorption and covalent linkage by benzoquinine.The experimental results show that the stability of PA is greatly increased,and the optimal temperature of PA is increased from 45 ℃ to 55 ℃.After thermal treatment at 50 ℃ for 25 h,the activity of immobilized enzyme remains 74.4%,maintaining 61.9% activity after repeated use for 15 times.

关 键 词：青霉素酰化酶 MCFs CLEA 对苯醌 

分 类 号：Q814.2[生物学—生物工程]