articleTop 10% cited
Preparation, optimization, and structures of cross‐linked enzyme aggregates (CLEAs)
Biotechnology and Bioengineering · 2004 · Vol. 87(6) · pp. 754–762
Rob Schoevaart(Delft University of Technology)M.W. Wolbers(Delft University of Technology)M. Golubovic(Delft University of Technology)Marcel Ottens(Delft University of Technology)A. P. G. Kieboom(Leiden University)Fred van Rantwijk(Delft University of Technology)Luuk A. M. van der Wielen(Delft University of Technology)Roger A. Sheldon✉(Delft University of Technology)
Abstract
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.
Enzyme Catalysis and ImmobilizationEnzyme-mediated dye degradationElectrochemical sensors and biosensorsYield (engineering)ChemistryEnzymeSimplicityBiochemical engineeringBiochemistryThermodynamicsPhysicsEngineering
MeSH terms
Cross-Linking ReagentsEnzyme ActivationEnzymesEnzymes, ImmobilizedFractional PrecipitationParticle SizeProtein ConformationMultiprotein Complexes
Citations
479
FWCI
4.32
field-weighted impact
References
26
Percentile
95%
vs. same field & year
Citations per year
Cited by
Cross-linked enzyme aggregates (CLEA®s): stable and recyclable biocatalysts
Biochemical Society Transactions · 2007 · 444 citations
References
Oxidation of non‐phenolic substrates
FEBS Letters · 1990 · 1,320 citations
Cross-Linked Enzyme Aggregates: A Simple and Effective Method for the Immobilization of Penicillin Acylase
Organic Letters · 2000 · 465 citations
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