| Autor: |
Kanzaki Y; Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan., Minami R; Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan., Ota K; Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan., Adachi J; Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan., Hori Y; Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan., Ohtani R; Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan., Le Ouay B; Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan., Ohba M; Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 819-0395, Japan. |
| Abstrakt: |
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. |
