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


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
Aantal pagina's15
ISBN van geprinte versie9780841225817
StatusGepubliceerd - 11 aug 2010
Extern gepubliceerdJa

Publicatie series

NaamACS Symposium Series
ISSN van geprinte versie00976156
ISSN van elektronische versie19475918


Duik in de onderzoeksthema's van 'Synthesis of covalently linked enzyme dimers sanne schoffelen1'. Samen vormen ze een unieke vingerafdruk.

Citeer dit