Physical, biochemical, and immunological characterization of a thermostable amidase from Klebsiella pneumoniae NCTR 1.

An amidase capable of degrading acrylamide and aliphatic amides was purified to apparent homogeneity from Klebsiella pneumoniae NCTR 1. The enzyme is a monomer with an apparent molecular weight of 62,000. The pH and temperature optima of the enzyme were 7.0 and 65 degrees C, respectively. The purifi...

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I whakaputaina i:	J Bacteriol
Ngā kaituhi matua:	Nawaz, M S, Khan, A A, Bhattacharayya, D, Siitonen, P H, Cerniglia, C E
Hōputu:	Artigo
Reo:	Inglês
I whakaputaina:	American Society for Microbiology (ASM) 1996
Ngā marau:	Research Article
Urunga tuihono:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC177951/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8636044/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.178.8.2397-2401.1996
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