4.6 Article

Polymer-Grafted 3D-Printed Material for Enzyme Immobilization-Designing a Smart Enzyme Carrier

Journal

CATALYSTS
Volume 13, Issue 7, Pages -

Publisher

MDPI
DOI: 10.3390/catal13071130

Keywords

additive manufacturing; surface-induced polymerization; stimuli-sensitive; polyacrylic acid; Esterase 2; CalB

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The flow properties of packed bed reactors can be enhanced using 3D printing to create optimized structures that improve mass transfer and catalyst conversion rates. Surface-induced polymerization can increase the number of enzymes and enable smart reaction control. This publication demonstrates the application of surface-induced polymerization on 3D-printed structures for enzyme carriers.
One way to enhance the flow properties of packed bed reactors, including efficient mass transfer and high catalyst conversion rates, is the use of 3D printing. By creating optimized structures that prevent channeling and high pressure drops, it is possible to achieve the desired target. Nevertheless, additively manufactured structures most often possess a limited surface-area-to-volume-ratio, especially as porous printed structures are not standardized yet. One way to achieve surface-enhanced 3D-printed structures is surface modification to introduce surface-initiated polymers. In addition, when stimuli-sensitive polymers are chosen, autonomous process control is prospective. The current publication deals with the application of surface-induced polymerization on 3D-printed structures with the subsequent application as an enzyme carrier. Surface-induced polymerization can easily increase the number of enzymes by a factor of six compared to the non-modified 3D-printed structure. In addition, the swelling behavior of polyacrylic acid is proven, even with immobilized enzymes, enabling smart reaction control. The maximum activity of Esterase 2 (Est2) from Alicyclobacillus acidocaldarius per g carrier, determined after 2 h of polymer synthesis, is 0.61 U/g(support). Furthermore, universal applicability is shown in aqueous and organic systems, applying an Est2 and Candida antarctica lipase B (CalB) catalyzed reaction and leaving space for improvement due to compatibility of the functionalization process and the here chosen organic solvent. Overall, no enzyme leaching is detectable, and process stability for at least five subsequent batches is ensured.

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