Laccase Encapsulation in ZIF-8 Metal-Organic Framework Shows Stability Enhancement and Substrate Selectivity

被引:43
|
作者
Knedel, Tim-Oliver [1 ]
Ricklefs, Esther [2 ]
Schluesener, Carsten [1 ]
Urlacher, Vlada B. [2 ]
Janiak, And Christoph [1 ]
机构
[1] Heinrich Heine Univ Dusseldorf, Inst Anorgan Chem & Strukturchem, D-40204 Dusseldorf, Germany
[2] Heinrich Heine Univ Dusseldorf, Inst Biochem, D-40204 Dusseldorf, Germany
来源
CHEMISTRYOPEN | 2019年 / 8卷 / 11期
关键词
laccase; metal-organic frameworks; ZIF-8; enzyme encapsulation; enzyme stabilization; substrate specificity; FACILE SYNTHESIS; IN-SITU; ENZYME; IMMOBILIZATION; SIZE; FUNGAL; TEMPERATURE; INDUSTRIAL; REDUCTION; WATER;
D O I
10.1002/open.201900146
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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 degrees 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%.
引用
收藏
页码:1337 / 1344
页数:8
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