天然矿物埃洛石为载体固定α-淀粉酶的工艺和性能(英文)  

TECHNOLOGY AND PERFORMANCE OF IMMOBILIZED α-AMYLASE BY HALLOYSITE

作　　者：杨方[1] 张冰[1] 刘金盾[1] 张浩勤[1] 乔梅英[1] 陈荣峰[2] 

机构地区：[1]郑州大学化学工程学院,郑州450001 [2]河南省科学院,郑州450002

出　　处：《硅酸盐学报》2008年第6期862-865,共4页Journal of The Chinese Ceramic Society

基　　金：河南省杰出青年基金(0612002400);国家博士后基金(060400789)资助项目

摘　　要：以天然纳米材料埃洛石为载体,通过物理吸附法对α-淀粉酶进行固定。利用红外光谱、扫描电镜、透射电镜等对埃洛石的结构和形貌特征进行测试与表征,同时对埃洛石纳米管固定化α-淀粉酶的条件及固定化酶的酶学性能进行了研究,并与游离酶进行了比较。结果表明:这种具有管状结构的埃洛石硅酸盐矿物是理想的酶载体,酶的固定化效率平均达到37.38%;所得的固定化α-淀粉酶4℃下保存15d后,酶活力仍保持90%以上;固定化α-淀粉酶的热稳定性也明显优于游离酶,连续7批次操作后仍保持56.2%的酶活力。Halloysite nanotubes, a new and economically viable material, were used to immobilize a-amylase by the physical adsorption method. The characteristics of the structure and morphology of the halloysite crystals were investigated by means of Fourier transform infrared spectroscopy, scanning electron microscope and transmission electron microscope. The properties of the immobi- lized enzyme were also investigated and compared with the free enzyme. It is demonstrated that the natural halloysite minerals are excellent supports for immobilizing enzymes. The immobilization efficiency of halloysite nanotubes is 37.38%, and higher than other supports under the same conditions. The thermal and storage stability of the immobilized a-amylase is much better than the free enzyme and the immobilized a-amylase could retain about 90% of the original activity for 15 d at 4 ℃. After seven times repeated batch operation, 56.2% relative activity of the immobilized a-amylase was retained, which demonstrated high operational stability.

关 键 词：埃洛石 物理吸附 固定化 Α-淀粉酶 管状结构 

分 类 号：TQ170.2[化学工程—硅酸盐工业]