| People | Locations | Statistics |
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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Hubbuch, Jürgen
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (12/12 displayed)
- 2023Standardized method for mechanistic modeling of multimodal anion exchange chromatography in flow through operationcitations
- 2022Systematic evaluation of agarose- and agar-based bioinks for extrusion-based bioprinting of enzymatically active hydrogelscitations
- 2022Synthesis of Spherical Nanoparticle Hybrids via Aerosol Thiol-Ene Photopolymerization and Their Bioconjugation
- 2020Straightforward method for calibration of mechanistic cation exchange chromatography models for industrial applicationscitations
- 2019Packing characteristics of winged shaped polymer fiber supports for preparative chromatographycitations
- 2019Water on hydrophobic surfaces: mechanistic modeling of polyethylene glycol-induced protein precipitation
- 2016A mechanistic model of ion-exchange chromatography on polymer fiber stationary phasescitations
- 2015Optimizing a chromatographic three component separation: A comparison of mechanistic and empiric modeling approachescitations
- 2015Examination of a genetic algorithm for the application in high-throughput downstream process developmentcitations
- 2015Model-integrated process development demonstrated on the optimization of a robotic cation exchange stepcitations
- 2015Determination of parameters for the steric mass action model - A comparison between experimental and modeling approachescitations
- 2015Detection, quantification, and propagation of uncertainty in high-throughput experimentation by Monte Carlo methodscitations
Places of action
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article
Systematic evaluation of agarose- and agar-based bioinks for extrusion-based bioprinting of enzymatically active hydrogels
Abstract
Extrusion-based 3D bioprinting enables the production of customized hydrogel structures that can be employed in flow reactors when printing with enzyme-containing inks. The present study compares inks based on either low-melt agarose or agar at different concentrations (3–6%) and loaded with the thermostable enzyme esterase 2 from the thermophilic organism Alicyclobacillus acidocaldarius (AaEst2) with regard to their suitability for the fabrication of such enzymatically active hydrogels. A customized printer setup including a heatable nozzle and a cooled substrate was established to allow for clean and reproducible prints. The inks and printed hydrogel samples were characterized using rheological measurements and compression tests. All inks were found to be sufficiently printable to create lattices without overhangs, but printing quality was strongly enhanced at 4.5% polymer or more. The produced hydrogels were characterized regarding mechanical strength and diffusibility. For both properties, a strong correlation with polymer concentration was observed with highly concentrated hydrogels being more stable and less diffusible. Agar hydrogels were found to be more stable and show higher diffusion rates than comparable agarose hydrogels. Enzyme leaching was identified as a major drawback of agar hydrogels, while hardly any leaching from agarose hydrogels was detected. The poor ability of agar hydrogels to permanently immobilize enzymes indicates their limited suitability for their employment in perfused biocatalytic reactors. Batch-based activity assays showed that the enzymatic activity of agar hydrogels was roughly twice as high as the activity of agarose hydrogels which was mostly attributed to the increased amount of enzyme leaching. Agarose bioinks with at least 4.5% polymer were identified as the most suitable of the investigated inks for the printing of biocatalytic reactors with AaEst2. Drawbacks of these inks are limited mechanical and thermal stability, not allowing the operation of a reactor at the optimum temperature of AaEst2 which is above the melting point of the employed low-melt agarose.