coupling of enzyme reaction to carbonyl reductase from Candida parapsilosis leads to total turnover numbers up to 143666 with maximum activity for NAD+ reduction at 35°C and pH 8.0. Half-life of enzyme is 5.3 h under these conditions. Presence of ammonium and potassium ions increases the enzyme stability
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
system for cloning and expression of multiple genes in Escherichia coli BL21 demonstrate tby production and maturation of the NAD+reducing soluble [NiFe]-hydrogenase from Cupriavidus necator H16. The enzyme encoded in hoxFUYHI is successfully matured by co-expression of a dedicated set of auxiliary genes, comprising seven hyp genes (hypC1D1E1A2B2F2X) along with hoxW, which encodes a specific endopeptidase. Deletion of genes involved in enzyme maturation reduces maturation efficiency substantially. Further addition of hoxN1, encoding a high-affinity nickel permease, considerably increases maturation efficiency in Escherichia coli
coupling of enzyme reaction to carbonyl reductase from Candida parapsilosis leads to total turnover numbers up to 143666 with maximum activity for NAD+ reduction at 35°C and pH 8.0. Half-life of enzyme is 5.3 h under these conditions. Presence of ammonium and potassium ions increases the enzyme stability
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