Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media

Hinzmann, Alessa; Stricker, Michael; Gröger, Harald

Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media

Hinzmann A, Stricker M, Gröger H (2020)
Catalysts 10(9): 1073.

Zeitschriftenaufsatz | Veröffentlicht | Englisch

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DOI

https://doi.org/10.3390/catal10091073

URN

urn:nbn:de:0070-pub-29461529

Autor*in

Hinzmann, Alessa^UniBi ; Stricker, Michael^UniBi; Gröger, Harald^UniBi

Einrichtung

Fakultät für Chemie > Industrielle Organische Chemie und Biotechnologie

Abstract / Bemerkung

Immobilization of biocatalysts is a current topic in research enabling the easy recovery of catalysts from the reaction medium after the reaction, and it is often accompanied by a stabilization of the catalysts, which enables recycling. Within our ongoing research on the utilization of aldoxime dehydratases in the cyanide-free synthesis of nitriles through dehydration of readily available aldoximes, a screening of different immobilization methods for free enzymes was performed. The applied immobilization methods are based on covalent binding and hydrophobic interactions of the enzyme with the carrier material and whole-cell immobilization in calcium alginate beads with and without subsequent coating. In our study, we found that the immobilization with purified free aldoxime dehydratases from OxdRE (Rhodococcus erythropolis) and OxdB (Bacillus sp. strain OxB-1) leads to high immobilization efficiencies, but also to a strong loss of activity with a residual activity of <20%, regardless of the carrier material used. However, when using whole cells for immobilization instead of purified enzymes, we could increase the residual activity significantly. Escherichia coli BL21(DE3)-CodonPlus-RIL OxdRE and OxdB whole cells were entrapped in calcium alginate beads and coated with silica using tetraethylorthosilicate (TEOS), leading to immobilized catalysts with up to 75% residual activity and a higher stability compared to the free whole cells. Even after three rounds of recycling, which corresponds to a 3 d reaction time, the immobilized OxdB whole cells showed a residual activity of 85%.

Stichworte

Physical and Theoretical Chemistry; Catalysis

Erscheinungsjahr

2020

Zeitschriftentitel

Catalysts

Band

Ausgabe

Art.-Nr.

1073

Urheberrecht / Lizenzen

Creative Commons Namensnennung 4.0 International Public License (CC-BY 4.0)

eISSN

2073-4344

Finanzierungs-Informationen

Open-Access-Publikationskosten wurden durch die Universität Bielefeld gefördert.

Page URI

https://pub.uni-bielefeld.de/record/2946152

Zitieren

Hinzmann A, Stricker M, Gröger H. Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media. Catalysts. 2020;10(9): 1073.

Hinzmann, A., Stricker, M., & Gröger, H. (2020). Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media. Catalysts, 10(9), 1073. https://doi.org/10.3390/catal10091073

Hinzmann, Alessa, Stricker, Michael, and Gröger, Harald. 2020. “Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media”. Catalysts 10 (9): 1073.

Hinzmann, A., Stricker, M., and Gröger, H. (2020). Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media. Catalysts 10:1073.

Hinzmann, A., Stricker, M., & Gröger, H., 2020. Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media. Catalysts, 10(9): 1073.

A. Hinzmann, M. Stricker, and H. Gröger, “Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media”, Catalysts, vol. 10, 2020, : 1073.

Hinzmann, A., Stricker, M., Gröger, H.: Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media. Catalysts. 10, : 1073 (2020).

Hinzmann, Alessa, Stricker, Michael, and Gröger, Harald. “Immobilization of Aldoxime Dehydratases and Their Use as Biocatalysts in Aqueous Reaction Media”. Catalysts 10.9 (2020): 1073.

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