碳酸酐酶在四氧化三铁上固定化及其性能表征研究  

An investigation of the immobilization of carbonic anhydrase on Fe_3O_4 and its performance characterization

作　　者：李娟[1] 周心澄[1] 张琳[1] 周磊[1] 杨林军[1] LI Juan ZHOU Xin-Cheng ZHANG Lin ZHOU Lei YANG Lin-Jun(Key Lab of Energy Thermal Conversion and Control of Ministry of Education, Southeast University, Nanjing 210096, China)

机构地区：[1]东南大学能源热转换及其过程测控教育部重点实验室,南京210096

出　　处：《四川大学学报（自然科学版）》2016年第6期1349-1354,共6页Journal of Sichuan University(Natural Science Edition)

基　　金：高等学校博士点专项科研基金(20130092110005);国家自然科学基金(51176034);东南大学优秀博士学位论文基金(YBJJ11508)

摘　　要：以四氧化三铁为载体,利用共价结合和交联法相结合的方法制备固定化碳酸酐酶(CA),通过单因素试验,得出CA最佳固定化条件,并对固定化酶进行性能表征.结果表明,在最优的固定化条件下,固定化酶的酶活回收率可达到66.90%,且其pH值稳定性、操作稳定性、热稳定性和贮藏稳定性明显高于同等条件下的游离酶,该固定化酶经5次催化水解底物后仍能保持62.58%的相对酶活.Carbonic anhydrase （CA） was immobilized on Fe304 by means of the covalent bonding and crosslinking method. The conditions of single factor, such as pH, temperature, time, shaker speed, en- zyme dose, glutaraldehyde dose, and glutaraldehyde time, were studied. And then the optimum condi- tions and properties of immobilization CA were obtained. The results showed that the rate of enzyme ac- tivity recovery of immobilized enzyme is 66.90% under the optimum conditions. And the pH stability, operational stability, thermal stability and storage stability of immobilized CA are significantly higher than that of the free CA. Particularly, the immobilized CA could keep 62.58% relative enzyme activity after 5 times of catalytic hydrolysis with the substrate.

关 键 词：碳酸酐酶(CA)固定化 CO2捕集 四氧化三铁 性能表征 

分 类 号：X511[环境科学与工程—环境工程]