Partial Purification and Characterization of a Thermostable Actinomycete β-Amylase
A thermostable amylase, possibly a β-amylase from Thermoactinomyces sp. no. 2 isolated from soil, is reported. The enzyme was purified 36-fold by acetone precipitation, ion-exchange chromatography, and Sephadex G-200 gel filtration, and the molecular weight was estimated at 31,600. The enzyme was ch...
Tallennettuna:
| Julkaisussa: | Appl Environ Microbiol |
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| Päätekijät: | , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
American Society for Microbiology (ASM)
1984
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC239722/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/16346495/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aem.47.3.571-575.1984 |
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