Preparation, optimization, and structures of cross-linked enzyme aggregates (CLEAs).
The broad applicability of the cross-linking of enzyme aggregates to the effective immobilisation of enzymes is demonstrated and the influence of many parameters on the properties of the resulting CLEAs is determined. The relative simplicity of the operation ideally lends itself to high-throughput methodologies. The aggregation method was improved up to 100% activity yield for any enzyme. For the first time, the physical structures of CLEAs are elucidated.
Biocatalysis and Organic Chemistry, Department of Biotechnology, Delft University of Technology, Julianalaan 136, 2628 BL, The Netherlands.
R
R
Schoevaart
M W
MW
Wolbers
M
M
Golubovic
M
M
Ottens
A P G
AP
Kieboom
F
F
van Rantwijk
L A M
LA
van der Wielen
R A
RA
Sheldon
D003432:Cross-Linking Reagents / Q000737:chemistry*; D004789:Enzyme Activation; D004798:Enzymes / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000302:isolation & purification / Q000648:ultrastructure; D005590:Fractional Precipitation; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure*; D010316:Particle Size; D011487:Protein Conformation
D003432:Cross-Linking Reagents; D004798:Enzymes; D004800:Enzymes, Immobilized; D046912:Multiprotein Complexes