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 m...

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Veröffentlicht in:	Biotechnology and bioengineering 2004-09, Vol.87 (6), p.754-762
Hauptverfasser:	Schoevaart, R., Wolbers, M.W., Golubovic, M., Ottens, M., Kieboom, A.P.G., van Rantwijk, F., van der Wielen, L.A.M., Sheldon, R.A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aggregates Biological and medical sciences Biotechnology CLEA CLEC Cross-Linking Reagents - chemistry Enzyme Activation Enzymes Enzymes - chemistry Enzymes - isolation & purification Enzymes - ultrastructure Enzymes, Immobilized - chemistry Enzymes, Immobilized - isolation & purification Enzymes, Immobilized - ultrastructure Fractional Precipitation Fundamental and applied biological sciences. Psychology Immobilization Immobilization of enzymes and other molecules Immobilization techniques Methods. Procedures. Technologies Multiprotein Complexes - chemistry Multiprotein Complexes - isolation & purification Multiprotein Complexes - ultrastructure Particle Size protein Protein Conformation Q1
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Zusammenfassung:	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. © 2004 Wiley Periodicals, Inc.
ISSN:	0006-3592 1097-0290
DOI:	10.1002/bit.20184