Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity
| Autor: | Carsten Schlüsener, Tim-Oliver Knedel, Esther Ricklefs, Christoph Janiak, Vlada B. Urlacher |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
substrate specificity
Composite number enzyme encapsulation 010402 general chemistry Heterogeneous catalysis 01 natural sciences Corynebacterium glutamicum laccase lcsh:Chemistry chemistry.chemical_compound metal-organic frameworks Laccase ABTS Aqueous solution Full Paper 010405 organic chemistry Chemistry fungi General Chemistry Full Papers 0104 chemical sciences Chemical engineering lcsh:QD1-999 enzyme stabilization Metal-organic framework Selectivity ZIF-8 |
| Zdroj: | ChemistryOpen, Vol 8, Iss 11, Pp 1337-1344 (2019) ChemistryOpen |
| ISSN: | 2191-1363 |
| Popis: | CgL1 laccase from Corynebacterium glutamicum was encapsulated into the metal‐organic framework (MOF) ZIF‐8 which was synthesized in a rapid enzyme friendly aqueous synthesis, the fastest in situ encapsulation of laccases reported to date. The obtained enzyme/MOF, i. e. laccase@ZIF‐8 composite showed enhanced thermal (up to 70 °C) and chemical (N,N‐dimethylformamide) stability, resulting in a stable heterogenous catalyst, suitable for high temperature reactions in organic solvents. Furthermore, the defined structure of ZIF‐8 produced a size selective substrate specificity, so that substrates larger than the pore size were not accepted. Thereby, 2’‐azino‐bis(3‐ethylbenzothiazoline‐6‐sulphonic acid) (ABTS) was used to verify that the enzyme is immobilized inside the MOF versus the outside surface. The enzyme@MOF composite was analyzed by atomic absorption spectroscopy (ASS) to precisely determine the enzyme loading to 2.1 wt%. |
| Databáze: | OpenAIRE |
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