Nanoporous Phyllosilicate Assemblies for Enzyme Immobilization

Shuang Mei; Jiafu Shi; Shaohua Zhang; Yue Wang; Yizhou Wu; Zhongyi Jiang; Hong Wu

doi:10.1021/acsabm.8b00642

Nanoporous Phyllosilicate Assemblies for Enzyme Immobilization

ACS Appl Bio Mater. 2019 Feb 18;2(2):777-786. doi: 10.1021/acsabm.8b00642. Epub 2019 Jan 28.

Authors

Shuang Mei^{1

2}, Jiafu Shi^{3

2

4}, Shaohua Zhang^{1

2}, Yue Wang¹, Yizhou Wu^{1

2}, Zhongyi Jiang^{1

3

2}, Hong Wu^{1

2

5}

Affiliations

¹ Key Laboratory for Green Chemical Technology of Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China.
² Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin 300072, China.
³ State Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, China.
⁴ School of Environment Science and Engineering, Tianjin University, Tianjin 300072, China.
⁵ Tianjin Key Laboratory of Membrane Science and Desalination Technology, Tianjin University, Tianjin 300072, China.

PMID: 35016282
DOI: 10.1021/acsabm.8b00642

Abstract

Physical/chemical adsorption is well-known as a facile and effective method for enzyme immobilization, while ideal adsorbents with a high structural stability, high loading capacity, and low leaching ratio are still under exploration. In this study, nanoporous assemblies of two-dimensional (2D) copper phyllosilicate (L-CuSiO₃) are prepared as an adsorbent to immobilize horseradish peroxidase (HRP) for phenol-containing wastewater treatment. Specifically, the robust chemical bonds of Si-O-Si and Si-O-Cu in L-CuSiO₃ ensure its superior structural stability; the well-developed porous structure endows L-CuSiO₃ assemblies with a high specific surface area of 611.7 cm³ g^-1, which enables a fast and high enzyme loading of 140 mg g^-1 within 4 h, and the well-distributed Cu(II) ions ensure the stable attachment of enzyme through Cu(II)-arginine (in HRP) coordination with a leaching ratio less than 10%. Meanwhile, the scaling assembly of L-CuSiO₃ renders the resultant biocatalyst (HRP-loaded L-CuSiO₃ assemblies) ease-of-recycling performance. Given the above features, the HRP-loaded L-CuSiO₃ assemblies exhibit a better stability and 2-fold higher activity by contrast with HRP adsorbed on conventional mesoporous SiO₂ and SiO₂ nanoparticles, and it also acted as an efficient bioreactor in the application of catalytical removal of phenol pollutants from wastewater. Our L-CuSiO₃ assemblies show great potential in immobilization of enzymes for industrial biocatalysis.

Keywords: Copper phyllosilicate (L-CuSiO3); enzyme immobilization; horseradish peroxidase; nanoporous assembly; phenol removal.