Enzyme-based inverse opals: a facile and promising platform for fabrication of biocatalysts

Yanjun Jiang; Cuicui Cui; Yan Huang; Xu Zhang; Jing Gao

doi:10.1039/c4cc01721h

Enzyme-based inverse opals: a facile and promising platform for fabrication of biocatalysts

Chem Commun (Camb). 2014 May 28;50(41):5490-3. doi: 10.1039/c4cc01721h.

Authors

Yanjun Jiang¹, Cuicui Cui, Yan Huang, Xu Zhang, Jing Gao

Affiliation

¹ School of Chemical Engineering and Technology, Hebei University of Technology, Tianjin 300130, P.R. China. xuzhang@hebut.edu.cn jgao@hebut.edu.cn.

PMID: 24722982
DOI: 10.1039/c4cc01721h

Abstract

A facile and promising approach was developed to fabricate enzyme-based 3D-ordered macroporous biocatalysts (enzyme-based inverse opals) by using the colloidal crystal templating method. Horseradish peroxidase- and amylase-based inverse opals were prepared, which verified that this method is suitable for various enzymes.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amylases / chemistry
Amylases / metabolism*
Animals
Biocatalysis*
Colloids / chemistry*
Enzyme Stability
Horseradish Peroxidase / chemistry
Horseradish Peroxidase / metabolism*
Models, Molecular
Molecular Conformation
Porosity
Temperature

Substances

Colloids
Horseradish Peroxidase
Amylases