Denaturation ofBacillus stearothermophilus ?-amylase by urea and detergents
| Autor: | W. Martin Teague, Phillip J. Brumm |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
chemistry.chemical_classification
Chromatography Bacillaceae biology chemistry.chemical_element Bioengineering General Medicine Calcium biology.organism_classification Applied Microbiology and Biotechnology Bacillales chemistry.chemical_compound Enzyme chemistry Biochemistry biology.protein Urea Denaturation (biochemistry) Amylase Bacteria Biotechnology |
| Zdroj: | Biotechnology Letters. 12:253-258 |
| ISSN: | 1573-6776 0141-5492 |
| DOI: | 10.1007/bf01093517 |
| Popis: | Denaturation ofBacillus stearothermophilus α-amylase by urea and detergents was investigated for the purpose of understanding the mechanism of denaturation of this enzyme. The enzyme was extremely resistant to denaturation by detergents at 60° C, either in the presence or absence of added calcium. Addition of EDTA was necessary to obtain denaturation by detergents. The rate of denaturation of the α-amylase by urea was strongly dependent on the incubation pH and presence or absence of calcium ions. Calcium-binding groups were shown to have pKa values of 5.5 for exogenous calcium and 4.7 to 4.8 for endogenous calcium. A mechanism is proposed for the denaturation ofBacillus stearothermophilus α-amylase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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