Reversible Supramolecular Surface Attachment of Enzyme–Polymer Conjugates for the Design of Biocatalytic Filtration Membranes. Issue 49 (13th October 2015)

• Record Type: Journal Article
• Authors: Moridi, Negar; Corvini, Philippe F.‐X.; Shahgaldian, Patrick
• Is Part Of: Angewandte Chemie international edition. Volume 54:Issue 49(2015)
• Page Start: 14800
• Page End: 14804
• Publication Date: 2015-10-13
• Subjects: enzyme catalysis -- polymers -- self‐assembly -- supramolecular chemistry -- surface chemistry; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201507020
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: To be used successfully in continuous reactor systems, enzymes must either be retained using filtration membranes or immobilized on a solid component of the reactor. Whereas the first approach requires large amounts of energy, the second approach is limited by the low temporal stability of enzymes under operational conditions. To circumvent these major stumbling blocks, we have developed a strategy that enables the reversible supramolecular immobilization of bioactive enzyme–polymer conjugates at the surface of filtration membranes. The polymer is produced through a reversible addition–fragmentation transfer method; it contains multiple adamantyl moieties that are used to bind the resulting conjugate at the surface of the membrane which has surface‐immobilized cyclodextrin macrocycles. This supramolecular modification is stable under operational conditions and allows for efficient biocatalysis, and can be reversed by competitive host–guest interactions. Abstract : Enzyme in the membrane : Supramolecular and reversible surface bioconjugation on a filtration membrane is achieved using a new enzyme–polymer conjugate containing multiple adamantyl units. As part of a membrane bioreactor this supramolecular modification is stable under operational conditions and allows for efficient biocatalysis.