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›› 2015, Vol. 15 ›› Issue (2): 336-340.

• 材料工程专栏 • 上一篇    下一篇

超细SiO2颗粒的制备及其对a-淀粉酶的吸附固定化

曹丽霞 王玲玲 刘会洲 杨传芳   

  1. 中国科学院过程工程研究所 中国科学院绿色过程与工程重点实验室 中国科学院过程工程研究所 中国科学院绿色过程与工程重点实验室 中国科学院过程工程研究所分离工程与工程青年实验室 中国科学院过程工程研究所分离工程与工程青年实验室
  • 收稿日期:2015-01-28 修回日期:2015-03-13 出版日期:2015-05-05 发布日期:2015-05-05
  • 通讯作者: 曹丽霞

Preparation of Ultrafine Silica Particles and Their Application in a-Amylase Immobilization

CAO Li-xia WANG Ling-ling LIU Hui-zhou YANG Chuan-fang   

  1. Key Laboratory of Green Process and Engineering, Institute of Process Engineering, Chinese Academy of Sciences Key Laboratory of Green Process and Engineering, Institute of Process Engineering, Chinese Academy of Sciences Institute of Process Engineering, Chinese Academy of Sciences Institute of Process Engineering, Chinese Academy of Sciences
  • Received:2015-01-28 Revised:2015-03-13 Online:2015-05-05 Published:2015-05-05
  • Contact: CAO Li-xia

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摘要： 采用TritonX-100反胶团体系法和St?ber法分别制备粒径为50 nm及1 μm的SiO2颗粒，用二氯二甲基硅烷(DDS)对其进行表面疏水性修饰，用于a-淀粉酶的固定化. 结果表明，经DDS修饰的SiO2颗粒对a-淀粉酶的吸附能力明显提高，且有效提高了吸附稳定性，经6次洗涤后酶活仅损失30%；1 μm SiO2颗粒比50 nm SiO2颗粒对a-淀粉酶的吸附量大，SiO2颗粒载体固定的a-淀粉酶的活性为50 nm SiO2>1 μm SiO2>50 nm修饰后SiO2>1 μm修饰后SiO2.

关键词: 超细SiO2颗粒, 二氯二甲基硅烷, a-淀粉酶, 固定化, 活性, 稳定性

Abstract: 50 nm and 1 mm SiO2 particles were prepared using TritonX-l00 reverse micellar system and St?ber method, respectively. The particles were then modified with dichlorodimethylsilane to render their surfaces hydrophobic for immobilization of a-amylase. The results showed that compared with unmodified SiO2 particles, the adsorption capacity of a-amylase on modified SiO2 particles was obviously improved, and the stability of immobilized a-amylase was also effectively increased, as evidenced by only 30% loss of activity after 6 times washing. The adsorption capacity of a-amylase on 1 μm SiO2 particles was higher than that on 50 nm SiO2 particles, while the activity of immobilized α-amylase on the different carriers was ranked in the order of 50 nm SiO2 > 1 mm SiO2 > modified 50 nm SiO2 > modified 1 mm SiO2.

Key words: ultrafine silica, dichlorodimethylsilane, a-amylase, immobilization, activity, stability

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