Immobilization and characterization of carbonic anhydrase on functionalized Fe3O4-SiO2 core-shell nanoparticles

NIU Jianjie; LIU Qi; ZHANG Shengwei; LYU Jing; LUO Dan; PENG Bo

doi:10.19666/j.rlfd.202007195

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Immobilization and characterization of carbonic anhydrase on functionalized Fe₃O₄-SiO₂ core-shell nanoparticles

更新时间：2025-09-28

- Immobilization and characterization of carbonic anhydrase on functionalized Fe₃O₄-SiO₂ core-shell nanoparticles
- Thermal Power Generation Vol. 50, Issue 1, Pages: 110-114(2021)
- 作者机构：
  
  1. 中国石油大学(北京)非常规油气科学技术研究院
  2. 中国石油大学(北京)温室气体封存与石油开采利用北京市重点实验室
  3. 中国石油大学(北京)新能源与材料学院
- 作者简介：
- 基金信息：
- DOI：10.19666/j.rlfd.202007195
  CLC： X511
- Published Online：30 December 2020，
  
  Published：2021
- 稿件说明：
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NIU Jianjie, LIU Qi, ZHANG Shengwei, et al. Immobilization and characterization of carbonic anhydrase on functionalized Fe₃O₄-SiO₂ core-shell nanoparticles[J]. Thermal power generation, 2021, 50(1): 110-114.
DOI：

NIU Jianjie, LIU Qi, ZHANG Shengwei, et al. Immobilization and characterization of carbonic anhydrase on functionalized Fe₃O₄-SiO₂ core-shell nanoparticles[J]. Thermal power generation, 2021, 50(1): 110-114. DOI： 10.19666/j.rlfd.202007195.

摘要

以Fe_3O_4纳米颗粒为核

正硅酸乙酯(TEOS)为前驱体

通过St?ber法合成了Fe_3O_4-SiO_2核壳纳米颗粒。以γ-缩水甘油醚氧丙基三甲氧基硅烷(GPTMS)为改性剂对纳米颗粒进行改性

得到了环氧基功能化的Fe_3O_4-SiO_2核壳纳米颗粒

随后将碳酸酐酶(carbonic anhydrase

CA)共价固定到纳米颗粒上

以实现CA固定化。采用傅立叶红外(FTIR)、透射电镜(TEM)等手段对载体材料进行表征;以对硝基苯酚乙酸酯(p-NPA)为底物

采用紫外分光光度仪测试酶活力

并对固定化酶进行了性能表征。试验结果表明

固定化酶的热稳定性、贮藏稳定性和循环使用性均优于同等条件下的游离酶

其在循环使用10次后仍保持84.2%的相对酶活力。

Abstract

The Fe_3O_4-SiO_2 core-shell nanoparticles were synthesized by a modified St?ber method using Fe_3O_4 nanoparticles as the core ethyl orthosilicate(TEOS) as a precursor. Fe_3O_4-SiO_2 core-shell nanoparticles were modified with 3-Glycidyloxypropyl trimethoxysilane to obtain epoxy-functionalized Fe_3O_4-SiO_2 core-shell nanoparticles

and then carbonic anhydrase(CA) was immobilized on the carrier material. The carrier material were characterized by Fourier transform infrared spectroscopy(FTIR) and transmission electron microscope(TEM). By using p-nitrophenol acetate(p-NPA) as a substrate

an ultraviolet spectrophotometer was used to test the enzyme activity

and the performance of immobilized enzyme was characterized. The results show that

the thermal stability

storage stability and recycling performance of the immobilized enzyme are better than the free enzyme under the same conditions

and it still maintains 84.2% relative activity after 10 times of recycling.

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