Loading...
Purification and characterization of a novel thermostable beta-amylase from Clostridium thermosulphurogenes.
An extracellular beta-amylase from Clostridium thermosulphurogenes was purified 811-fold to homogeneity, and its general molecular, physico-chemical and catalytic properties were determined. The native enzyme was a tetramer of 210 kDa composed of a single type subunit; its 20 amino acid N-terminus d...
Na minha lista:
| Main Authors: | , , , , |
|---|---|
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
1988
|
| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1135158/ https://ncbi.nlm.nih.gov/pubmed/2461701 |
| Tags: |
Tilføj Tag
Ingen Tags, Vær først til at tagge denne postø!
|