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...
Αποθηκεύτηκε σε:
| Εκδόθηκε σε: | Appl Environ Microbiol |
|---|---|
| Κύριος συγγραφέας: | |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
American Society for Microbiology (ASM)
1993
|
| Θέματα: | |
| Διαθέσιμο Online: | 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 |
| Ετικέτες: |
Δεν υπάρχουν, Καταχωρήστε ετικέτα πρώτοι!
|