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Strategy for the isolation of native dehydrogenases with potential for biosensor development from the organism Hyphomicrobium zavarzinii ZV580

Titelangaben

Hilbrig, Frank ; Jérôme, Valérie ; Salzig, Mark ; Freitag, Ruth:
Strategy for the isolation of native dehydrogenases with potential for biosensor development from the organism Hyphomicrobium zavarzinii ZV580.
In: Journal of Chromatography A. Bd. 1216 (2009) Heft 16 . - S. 3518-3525.
ISSN 0021-9673
DOI: https://doi.org/10.1016/j.chroma.2008.09.020

Volltext

Link zum Volltext (externe URL): Volltext

Abstract

Dehydrogenases are interesting candidates for the development of electrochemical biosensors. Most dehydrogenases are characterised by a comparatively broad substrate spectrum, yet highly specific enzymes exist as well. A specific formaldehyde dehydrogenase has, e.g., been described for the organism Hyphomicrobium zavarzinii ZV580. Isolation of enzymes from their natural source instead of a recombinant expression renders the isolation more challenging, as common tools such as affinity tags are no longer available. In this contribution, we develop chromatographic procedures for such isolation tasks. The previously described formaldehyde dehydrogenase was isolated by two procedures, one based on affinity chromatography, the other on hydroxyapatite. Neither procedure yielded an active enzyme. In addition two dehydrogenases, a formaldehyde and a methylamine dehydrogenase, were found in the cell free extract, which had not been described previously. Both enzymes could be isolated to near purity by a sequence of hydroxyapatite and anion exchange chromatography. The new formaldehyde dehydrogenase requires reconstitution with calcium and pyrroloquinoline quinone in order to become active. The enzyme shows no cross-reactivity with methylamine or methanol. The methylamine dehydrogenase catalyses the conversion of methylamine into formaldehyde, hence it could become a technical catalyst for the inverse reaction. This enzyme consists of two types of subunit and may be one of the rare α,β-methylamine dehydrogenases.

Weitere Angaben

Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Zusätzliche Informationen: 32nd International Symposium on High Performance Liquid Phase Separations and Related Techniques
Keywords: Hyphomicrobium zavarzinii
Institutionen der Universität: Fakultäten > Fakultät für Ingenieurwissenschaften
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Bioprozesstechnik
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Bioprozesstechnik > Lehrstuhl Bioprozesstechnik - Univ.-Prof. Dr. Ruth Freitag
Fakultäten
Titel an der UBT entstanden: Ja
Themengebiete aus DDC: 600 Technik, Medizin, angewandte Wissenschaften
600 Technik, Medizin, angewandte Wissenschaften > 620 Ingenieurwissenschaften
Eingestellt am: 24 Feb 2016 13:41
Letzte Änderung: 30 Jun 2022 10:21
URI: https://eref.uni-bayreuth.de/id/eprint/31036