Related Experiment Video
Updated: Jun 12, 2025

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
Published on: February 5, 2020
Enhancing Performances of Enzyme/Metal-Organic Polyhedra Composites by Mixed-Protein Co-Immobilization
Yuri Kanzaki1, Ryosuke Minami1, Koshiro Ota1
1Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan.
Abstract:
Protein immobilization using water-soluble ionic metal-organic polyhedra (MOPs) acting as porous spacers has recently been demonstrated as a potent strategy for the preparation of biocatalysts. In this article, we describe a mixed-protein approach to achieve biocomposites with adjustable enzyme contents and excellent immobilization efficiencies, in a systematic and well-controlled manner. Self-assembly of either cationic or anionic MOPs with bovine serum albumin or egg white lysozyme combined with enzymes (alkaline phosphatase, laccase or cytochrome c) led to solid-state catalysts with a high retention of enzyme activity. Furthermore, for all these systems, the dilution of enzymes within the solid-state composite led to noticeably improved catalytic performances, with both higher specific activity and affinity for substrate.
Related Concept Videos
Complexation Equilibria: The Chelate Effect
Complexometric Titration: Ligands
Metal-Ligand Bonds
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
EDTA: Chemistry and Properties

