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  4. Enzyme immobilization on synthesized nanoporous silica particles and their application in a bi-enzymatic reaction
 
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Enzyme immobilization on synthesized nanoporous silica particles and their application in a bi-enzymatic reaction

Citation Link: https://doi.org/10.15480/882.2748
Publikationstyp
Journal Article
Date Issued
2020-01-27
Sprache
English
Author(s)
Engelmann, Claudia  
Ekambaram, Narendhiran  
Johannsen, Jens  orcid-logo
Fellechner, Oliver 
Waluga, Thomas  
Fieg, Georg  
Liese, Andreas  orcid-logo
Bubenheim, Paul  orcid-logo
Institut
Technische Biokatalyse V-6  
Prozess- und Anlagentechnik V-4  
Thermische Verfahrenstechnik V-8  
TORE-DOI
10.15480/882.2748
TORE-URI
http://hdl.handle.net/11420/5891
Journal
ChemCatChem  
Volume
12
Issue
8
Start Page
2245
End Page
2252
Citation
ChemCatChem 8 (12): 2245-2252 (2020)
Publisher DOI
10.1002/cctc.201902293
Scopus ID
2-s2.0-85080130268
Publisher
WILEY-VCH Verlag
The application of enzymes presents a great advantage regarding highly selective reactions; however, it involves also challenges due to their sensitivity. Immobilization offers one strategy to overcome those challenges enabling enzyme stabilization, as well as retention. In the present study, covalent attachment on hydrophilic amino-functionalized carriers is found to be the most promising immobilization method for the investigated reaction system. To achieve this, a novel method for preparation of silica particles with subsequent amino-functionalization is developed to prepare spherical carriers for enzyme immobilization, whereby high porosities are obtained based on polymerization. With these particles, immobilization of an alcohol dehydrogenase and a formate dehydrogenase is realized with residual activities of 70 and 80 % after 12 consecutive batches, respectively. The two immobilized enzymes are used in the reduction of cinnamyl aldehyde with in situ cofactor regeneration, obtaining a conversion of 100 % and up to 10-fold higher turnover numbers compared to the free enzyme.
Subjects
Alcohol dehydrogenase
Aromatic compounds
Biocatalysis
Cofactor regeneration
Immobilization
DDC Class
600: Technik
Funding(s)
Multienzymkaskade im 2-Phasensystem  
Projekt DEAL  
More Funding Information
Supported by Deutsche Forschungsgemeinschaft (DFG, BU 3409/1-1 and DFG, WA 3957/1-1)
Lizenz
https://creativecommons.org/licenses/by/4.0/
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