Scinovex
articleTop 10% cited

Preparation, optimization, and structures of cross‐linked enzyme aggregates (CLEAs)

Biotechnology and Bioengineering · 2004 · Vol. 87(6) · pp. 754–762
Rob SchoevaartM.W. WolbersM. GolubovicMarcel OttensA. P. G. KieboomFred van RantwijkLuuk A. M. van der WielenRoger A. Sheldon

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
Citation Network

How this paper connects to the literature. Drag to explore, click any node to open that paper.

Preparation, optimization, and structures of cross‐linked enzyme aggregates (CLEAs) · Scinovex