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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...
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| Главные авторы: | , , , , |
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| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
1988
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1135158/ https://ncbi.nlm.nih.gov/pubmed/2461701 |
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