l-Selective Amidase with Extremely Broad Substrate Specificity from Ochrobactrum anthropi NCIMB 40321

An industrially attractive l-specific amidase was purified to homogeneity from Ochrobactrum anthropi NCIMB 40321 wild-type cells. The purified amidase displayed maximum initial activity between pH 6 and 8.5 and was fully stable for at least 1 h up to 60°C. The purified enzyme was strongly inhibited...

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Autores principales: Sonke, Theo, Ernste, Sandra, Tandler, Renate F., Kaptein, Bernard, Peeters, Wilco P. H., van Assema, Friso B. J., Wubbolts, Marcel G., Schoemaker, Hans E.
Formato: Artigo
Lenguaje:Inglês
Publicado: American Society for Microbiology 2005
Materias:
Enzymology and Protein Engineering
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1317364/
https://ncbi.nlm.nih.gov/pubmed/16332774
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.71.12.7961-7973.2005
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