Purification and Characterization of an l-Amino Amidase from Mycobacterium neoaurum ATCC 25795

An l-amino amidase from Mycobacterium neoaurum ATCC 25795 responsible for the enantioselective resolution of dl-α-methyl valine amide was purified and characterized. The purification procedure included ammonium sulfate fractionation, gel filtration, and anion-exchange chromatography, which resulted...

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Библиографические подробности

Опубликовано в::	Appl Environ Microbiol
Главные авторы:	Hermes, H. F. M., Tandler, R. F., Sonke, T., Dijkhuizen, L., Meijer, E. M.
Формат:	Artigo
Язык:	Inglês
Опубликовано:	American Society for Microbiology (ASM) 1994
Предметы:	Enzymology and Protein Engineering
Online-ссылка:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC201283/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/16349147/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.60.1.153-159.1994
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