Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity
Abstract 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 composi...
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| Format: | Article |
| Language: | English |
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Wiley-VCH
2019-11-01
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| Series: | ChemistryOpen |
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| Online Access: | https://doi.org/10.1002/open.201900146 |
| _version_ | 1818940522246438912 |
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| author | Tim‐Oliver Knedel Dr. Esther Ricklefs Carsten Schlüsener Prof. Dr. Vlada B. Urlacher Prof. Dr. Christoph Janiak |
| author_facet | Tim‐Oliver Knedel Dr. Esther Ricklefs Carsten Schlüsener Prof. Dr. Vlada B. Urlacher Prof. Dr. Christoph Janiak |
| author_sort | Tim‐Oliver Knedel |
| collection | DOAJ |
| description | Abstract 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%. |
| first_indexed | 2024-12-20T06:40:59Z |
| format | Article |
| id | doaj.art-a92add6294e44c7abe4f466e8a78afd5 |
| institution | Directory Open Access Journal |
| issn | 2191-1363 |
| language | English |
| last_indexed | 2024-12-20T06:40:59Z |
| publishDate | 2019-11-01 |
| publisher | Wiley-VCH |
| record_format | Article |
| series | ChemistryOpen |
| spelling | doaj.art-a92add6294e44c7abe4f466e8a78afd52022-12-21T19:49:51ZengWiley-VCHChemistryOpen2191-13632019-11-018111337134410.1002/open.201900146Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate SelectivityTim‐Oliver Knedel0Dr. Esther Ricklefs1Carsten Schlüsener2Prof. Dr. Vlada B. Urlacher3Prof. Dr. Christoph Janiak4Institut für Anorganische Chemie und Strukturchemie Heinrich-Heine-Universität Düsseldorf 40204 DüsseldorfInstitut für Biochemie Heinrich-Heine-Universität Düsseldorf 40204 DüsseldorfInstitut für Anorganische Chemie und Strukturchemie Heinrich-Heine-Universität Düsseldorf 40204 DüsseldorfInstitut für Biochemie Heinrich-Heine-Universität Düsseldorf 40204 DüsseldorfInstitut für Anorganische Chemie und Strukturchemie Heinrich-Heine-Universität Düsseldorf 40204 DüsseldorfAbstract 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%.https://doi.org/10.1002/open.201900146laccasemetal-organic frameworksZIF-8enzyme encapsulationenzyme stabilizationsubstrate specificity |
| spellingShingle | Tim‐Oliver Knedel Dr. Esther Ricklefs Carsten Schlüsener Prof. Dr. Vlada B. Urlacher Prof. Dr. Christoph Janiak Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity ChemistryOpen laccase metal-organic frameworks ZIF-8 enzyme encapsulation enzyme stabilization substrate specificity |
| title | Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity |
| title_full | Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity |
| title_fullStr | Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity |
| title_full_unstemmed | Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity |
| title_short | Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity |
| title_sort | laccase encapsulation in zif 8 metal organic framework shows stability enhancement and substrate selectivity |
| topic | laccase metal-organic frameworks ZIF-8 enzyme encapsulation enzyme stabilization substrate specificity |
| url | https://doi.org/10.1002/open.201900146 |
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