Literature summary for 1.12.1.2 extracted from

Herr, N.; Ratzka, J.; Lauterbach, L.; Lenz, O.; Ansorge-Schumacher, M.
Stability enhancement of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase by a combination of immobilisation and chemical modification (2013), J. Mol. Catal. B, 97, 169-174.

No PubMed abstract available

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Application

Application	Comment	Organism
synthesis	immobilization of enzyme onto the anionic resin AmberliteTMFPA54 with immobilisation yield of 93.4% for adsorptive and 100% forcovalent attachment, corresponding activities of 48.9 and 39.3%, respectively, leading to stabilisation of enzyme. At elevated temperature and under agitation, stabilisation is further increased by modification of the covalently bound SH with methoxy-poly(ethylene) glycol(mPEG). In stationary aqueous solution, half-lives of up to 161 h at 25°C and 32 h at 35°C are obtained.In presence of the DMSO, DMF, 2-propanol and [EMIM][EtSO4] half-lives of 14-29 h can be achieved	Cupriavidus necator

Cloned(Commentary)

Cloned (Comment)	Organism
over-expression of a plasmid carrying the hoxFUYWI-hypA2B2F2CDEXA genes in Cupriavidus necator	Cupriavidus necator

Organism

Organism	UniProt	Comment	Textmining
Cupriavidus necator	-	-	-
Cupriavidus necator DSM 428	-	-	-

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
35	-	pH 8.0, native enzyme, half-life 5.3 h	Cupriavidus necator

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Release 2023.1 (January 2023)