Purification and Characterization of d-Aminoacylase from Alcaligenes faecalis DA1

A d-aminoacylase from Alcaligenes faecalis DA1 has been purified to homogeneity by a simple purification procedure with two columns, Fractogel DEAE-650 and HW-50. The specific activity of the purified enzyme was found to be 580 U/mg of protein with N-acetyl-dl-methionine as the reaction substrate. T...

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Vydáno v:	Appl Environ Microbiol
Hlavní autoři:	Yang, Yunn-Bor, Lin, Chyuan-Sheng, Tseng, Ching-Ping, Wang, Yng-Jiin, Tsai, Ying-Chieh
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1991
Témata:	Enzymology and Protein Engineering
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC182879/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/16348465/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.57.4.1259-1260.1991
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