Synthesis of covalently linked enzyme dimers sanne schoffelen1

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

Research output: Chapter in Book/Report/Conference proceedingConference contributionAcademicpeer-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.

Original languageEnglish
Title of host publicationGreen Polymer Chemistry: Biocatalysis and Biomaterials
PublisherAmerican Chemical Society
Number of pages15
ISBN (Print)9780841225817
Publication statusPublished - 11 Aug 2010
Externally publishedYes

Publication series

NameACS Symposium Series
ISSN (Print)00976156
ISSN (Electronic)19475918


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