Open AccessCover Feature: Laccase Encapsulation in ZIF‐8 Metal‐Organic Framework Shows Stability Enhancement and Substrate Selectivity (ChemistryOpen 11/2019)
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.201900308
Subject(s) - laccase , selectivity , substrate (aquarium) , thermal stability , chemistry , chemical engineering , metal organic framework , encapsulation (networking) , materials science , nanotechnology , combinatorial chemistry , enzyme , organic chemistry , catalysis , computer science , computer network , adsorption , oceanography , engineering , geology
The Cover Feature shows a schematic presentation of laccase enzyme molecules encapsulated in the metal organic framework ZIF‐8. The composite was synthesized in situ and enzyme friendly with the fastest encapsulation method reported to this day, thereby bypassing the problem of the enzyme being larger than the pore windows. Laccase@ZIF‐8 showed enhanced thermal and chemical stability, along with substrate specificity caused by the small pore windows of the ZIF‐8 MOF. Small substrates like 2,6‐dimethoxyphenol and syringaldazine are converted, whereas the larger substrate ABTS is not accepted. The latter also indicates the enzyme being entrapped in the pores and not simply immobilized on the MOF‐surface. More information can be found in the Full Paper by T.‐O. Knedel et al. on page 1337 in Issue 11, 2019 (DOI: 10.1002/open.201900146).