Polymer-grafted 3D-printed material for enzyme immobilization : designing a smart enzyme carrier

Publikationstyp
Journal Article
Date Issued
2023-07-20
Sprache
English
Author(s)
Eixenberger, Daniela 
Technische Biokatalyse V-6  
Kumar, Aditya  
Klinger, Saskia
Scharnagl, Nico  
Dawood, Ayad 
Technische Biokatalyse V-6  
Liese, Andreas  orcid-logo
Technische Biokatalyse V-6  
TORE-DOI
10.15480/882.8045
TORE-URI
https://hdl.handle.net/11420/42396
Journal
Catalysts  
Volume
13
Issue
7
Article Number
1130
Citation
Catalysts 13 (7): 1130 (2023)
Publisher DOI
10.3390/catal13071130
Scopus ID
2-s2.0-85166344468
Publisher
Multidisciplinary Digital Publishing Institute
Peer Reviewed
true
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.
Subjects
additive manufacturing
surface-induced polymerization
stimuli-sensitive
polyacrylic acid
Esterase 2
CalB
DDC Class
540: Chemistry
570: Life Sciences, Biology
Publication version
publishedVersion
Lizenz
https://creativecommons.org/licenses/by/4.0/
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