The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Preparation, optimization, and structures of cross‐linked enzyme aggregates (CLEAs)
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. © 2004 Wiley Periodicals, Inc.
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Self-citationINTERMOLECULAR CROSS LINKING OF A PROTEIN IN THE CRYSTALLINE STATE: CARBOXYPEPTIDASE-A
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Self-citationCross-linked enzyme aggregates (CLEA®s): stable and recyclable biocatalysts
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Bioinspired enzyme encapsulation for biocatalysis
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Bilal, M., Asgher, M., Parra-Saldivar, R., Hu, H., Wang, W., Zhang, X., & Iqbal, H. M. N. (2017) · Science of The Total Environment · doi:10.1016/j.scitotenv.2016.10.137 · Cited by 382
Metadata
- Authors
- 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.
- Venue
- Biotechnology and Bioengineering
- Publisher
- Wiley
- Published
- 2004-08-19
- Volume
- 87
- Issue
- 6
- Pages
- 754-762
- ISSN
- 0006-3592 (ISSN-L)
- 1097-0290
- OpenAlex
- W2030974312
- Cited by
- 485
- References
- 18
- FWCI
- 3.94
- Type
- journal article
- Language
- en
- Open access
- closed
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