Acta Chimica Sinica ›› 2021, Vol. 79 ›› Issue (12): 1502-1510.DOI: 10.6023/A21080385 Previous Articles     Next Articles



高霞a,*(), 潘会宾b, 贺曾贤a, 杨柯a, 乔成芳a, 刘永亮a, 周春生a   

  1. a 商洛学院化学工程与现代材料学院 陕西省尾矿资源综合利用重点实验室 商洛 726000
    b 商洛职业技术学院公共课教学部 商洛 726000
  • 投稿日期:2021-08-16 发布日期:2021-10-08
  • 通讯作者: 高霞
  • 基金资助:
    国家自然科学基金(22003037); 国家自然科学基金(22173056); 陕西省教育厅重点实验室项目(20JS043); 商洛学院自然科学基金项目(19SKY003); 商洛学院自然科学基金项目(20SKY005); 商洛学院科研团队项目(20SCX01)

Construction and Structure-Activity Relationship of Immobilized Enzyme Reactor Based on Al-MOF-Derived Al2O3 with Hierarchical Structure

Xia Gaoa(), Huibin Panb, Zengxian Hea, Ke Yanga, Chengfang Qiaoa, Yongliang Liua, Chunsheng Zhoua   

  1. a Shaanxi Key Laboratory of Comprehensive Utilization of Tailings Resources, School of Chemical Engineering & Modern Materials, Shangluo University, Shangluo 726000, China
    b Department of Public Education, Shangluo Vocational & Technical College, Shangluo 726000, China
  • Received:2021-08-16 Published:2021-10-08
  • Contact: Xia Gao
  • Supported by:
    National Natural Science Foundation of China(22003037); National Natural Science Foundation of China(22173056); Key Laboratory Project of Education Department of Shaanxi Province(20JS043); Natural Science Foundation Project(19SKY003); Natural Science Foundation Project(20SKY005); Scientific Research Team Project(20SCX01)

Although enzyme catalysis has many advantages such as green, high efficiency and so on, the industrial application of enzyme is often hampered by a lack of long-term operational stability and difficult to re-use. These drawbacks can generally be overcome by immobilization of the enzyme on a solid carrier. However, the immobilized enzyme reactor often can not remain all the initial catalytic activity due to the enzyme shedding during reuse, change of conformation and the difficulty for substrates to access the active site of enzyme in the carrier, etc. The contradiction between catalytic activity and stability of biological enzyme molecules supported on solid phase carriers has become a bottleneck in the design and preparation of immobilized enzyme reactors. Therefore, it is a challenging task to construct an immobilized enzyme reactor with both high catalytic activity and high stability. In this work, aluminum-based metal-organic framework (Al-MOF)-derived hierarchical porous Al2O3 (MHAl2O3) was prepared by the self-sacrificial template strategy and functionally modified with “polydopamine (PDA)” bionic membrane for entrapping horseradate peroxidase (HRP). The pore size was regulated by changing the calcination temperature of precursor. The influence of channel confinement effect of the carrier on the catalytic activity of the enzyme reactor was discussed, and the thermal stability and reusability of the HRP@PDA@MHAl2O3 was significantly improved. After 1 h at 70 ℃, 98.5% of the catalytic activity of HRP@PDA@MHAl2O3 could be maintained. After 10 times of reuse, 90.9% of the catalytic activity was still maintained. In order to analyze the structure-activity relationship of the enzyme reactor, the interaction between enzyme and substrate in the reaction catalyzed by HRP@PDA@MHAl2O3 was studied by means of enzyme kinetics and thermodynamic parameters, which showed that the affinity and specificity of the enzyme to the substrate were improved. When the enzyme reactor was applied to the catalytic degradation of aniline aerofloat in simulated wastewater, the degradation rate of 40 mg•L-1 substrate in 30 min reached 82.7% under the best reaction conditions.

Key words: metal-organic framework (MOF), horseradish peroxidase, immobilized enzyme reactor, enzyme catalysis, structure-activity relationship