Open AccessLaccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity
Author(s) -
Knedel TimOliver,
Ricklefs Esther,
Schlüsener Carsten,
Urlacher Vlada B.,
Janiak Christoph
Publication year - 2019
Publication title -
chemistryopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.644
H-Index - 29
ISSN - 2191-1363
DOI - 10.1002/open.201900146
Subject(s) - laccase , metal organic framework , chemistry , selectivity , abts , thermal stability , immobilized enzyme , chemical engineering , aqueous solution , substrate (aquarium) , catalysis , combinatorial chemistry , organic chemistry , enzyme , adsorption , engineering , oceanography , antioxidant , dpph , geology
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%.