General Properties of Beta-Galactosidase of Xanthomonas campestris
Partially purified β-galactosidase of Xanthomonas campestris required 32 to 37°C and pH 5.5 to 5.8 for optimum activity. The enzyme had low affinity for lactose hydrolysis (K(m) = 22 mM) and was inhibited by thiol group reagents, ethylenediaminetetraacetic acid, galactose, and d-galactal.
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| Опубликовано в:: | Appl Environ Microbiol |
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| Главные авторы: | , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
American Society for Microbiology (ASM)
1979
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC243532/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/16345439/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.38.3.554-556.1979 |
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