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...
Збережено в:
| Опубліковано в:: | J Bacteriol |
|---|---|
| Автори: | , , , , |
| Формат: | Artigo |
| Мова: | Inglês |
| Опубліковано: |
American Society for Microbiology (ASM)
1996
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| Предмети: | |
| Онлайн доступ: | 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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