Synthesis of covalently linked enzyme dimers sanne schoffelen1

L. Schobers, H. Venselaar, Gert Vriend, J.C.M. Hest, van

Onderzoeksoutput: Hoofdstuk in Boek/Rapport/CongresprocedureConferentiebijdrageAcademicpeer review

Samenvatting

The covalent linkage of enzymes that collaborate in a multistep reaction may have a beneficial effect on substrate conversion. Site-specific modification strategies ensure absolute control over the site of coupling. We show that well-defined enzyme architectures can be prepared via site-specific incorporation of novel functionalities into the model enzyme Candida Antarctica Lipase B (CalB). Different kinds of dimers were produced in which the covalent connection brought both active sites or both N-termini in proximity of each other. Dimers were as active as their respective monomers, both towards monofunctional substrates and molecules containing two substrate moieties.

Originele taal-2Engels
TitelGreen Polymer Chemistry: Biocatalysis and Biomaterials
UitgeverijAmerican Chemical Society
Pagina's125-139
Aantal pagina's15
Volume1043
ISBN van geprinte versie9780841225817
DOI's
StatusGepubliceerd - 11 aug 2010
Extern gepubliceerdJa

Publicatie series

NaamACS Symposium Series
Volume1043
ISSN van geprinte versie00976156
ISSN van elektronische versie19475918

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  • Citeer dit

    Schobers, L., Venselaar, H., Vriend, G., & Hest, van, J. C. M. (2010). Synthesis of covalently linked enzyme dimers sanne schoffelen1. In Green Polymer Chemistry: Biocatalysis and Biomaterials (Vol. 1043, blz. 125-139). (ACS Symposium Series; Vol. 1043). American Chemical Society. https://doi.org/10.1021/bk-2010-1043.ch010