Purification and characterization of the extracellular alpha-amylase from Streptococcus bovis JB1.
The extracellular alpha-amylase (1,4-alpha-D-glucanglucanohydrolase; EC 3.2.1.1) from maltose-grown Streptococcus bovis JB1 was purified to apparent homogeneity by ion-exchange chromatography (Mono Q). The enzyme had an isoelectric point of 4.50 and an apparent molecular mass of 77,000 Da, as estima...
Tallennettuna:
| Julkaisussa: | Appl Environ Microbiol |
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| Päätekijä: | |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
American Society for Microbiology (ASM)
1993
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC182095/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8517735/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.59.5.1398-1402.1993 |
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