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Simple Enzyme Immobilization for Flow Chemistry? An Assessment of Available Strategies for an Acetaldehyde-Dependent Aldolase

ORCID
0000-0001-7001-7412
Affiliation
Institute for Bioorganic Chemistry, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany
Wäscher, Martin;
ORCID
0000-0002-3259-964X
Affiliation
Institute for Bio- and Geosciences 1: Bioorganic Chemistry, Forschungszentrum Jülich, 52425 Jülich, Germany
Classen, Thomas;
ORCID
0000-0002-9819-889X
Affiliation
Institute for Bioorganic Chemistry, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany
Pietruszka, Jörg

Enzyme immobilization is a technology that enables (bio-)catalysts to be applied in continuous-flow systems. However, there is a plethora of immobilization methods available with individual advantages and disadvantages. Here, we assessed the influence of simple and readily available methods with respect to the performance of 2-deoxy- d -ribose-5-phosphate aldolase (DERA) in continuous-flow conditions. The investigated immobilization strategies cover the unspecific attachment to carriers via epoxides, affinity-based attachment via metal ion affinity, StrepTag™-StrepTactin™ interaction as well as the covalent affinity attachment of an enzyme to a matrix tethered by the HaloTag ® . The metal-ion-affinity-based approach outperformed the other methods in terms of immobilized activity and stability under applied conditions. As most enzymes examined today already have a HisTag for purification purposes, effective immobilization may be applied, as simple as a standard purification, if needed.

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