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Inside Cover: Oriented Immobilization of Enzymes Made Fit for Applied Biocatalysis: Non‐Covalent Attachment to Anionic Supports using Z basic2 Module (ChemCatChem 8/2011)
Author(s) -
Wiesbauer Johanna,
Bolivar Juan M.,
Mueller Mario,
Schiller Margaretha,
Nidetzky Bernd
Publication year - 2011
Publication title -
chemcatchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201190033
Subject(s) - biocatalysis , covalent bond , leuconostoc mesenteroides , chemistry , immobilized enzyme , ionic bonding , cover (algebra) , enzyme , ionic liquid , thio , enzyme catalysis , catalysis , chemical engineering , combinatorial chemistry , organic chemistry , mechanical engineering , lactic acid , ion , engineering , genetics , biology , bacteria
The inside cover picture shows the structural model of sucrose phosphorylase from Leuconostoc mesenteroides fused to a positively charged Z basic2 module that is placed next to a carrier surface showing the opposing (negative) charge. In their Communication on p. 1299 ff. , B. Nidetzky et al., describe that non‐covalent attachment to ionic supports is a very useful approach for a reversible oriented immobilization of a number of enzymes. High protein loading and excellent catalytic effectiveness of the carrier‐bound enzymes can be achieved.