Characterisation of a thermostable alpha-amylase from Bacillus brevis
| Autor: | E. Emanuilova, M. Stefanova |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
Hot Temperature Chromatography biology Starch Carbohydrates Bacillus Biochemistry Substrate Specificity Kinetics Hydrolysis chemistry.chemical_compound Enzyme chemistry Amylose Amylopectin Enzyme Stability biology.protein Thermodynamics Amylase Amino Acids alpha-Amylases Alpha-amylase Thermostability |
| Zdroj: | European Journal of Biochemistry. 207:345-349 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1992.tb17056.x |
| Popis: | Biochemical characterization of a novel heat-stable alpha-amylase, produced by a thermophilic strain of Bacillus brevis, has been made. The pattern of the enzyme action on different substrates was studied. It was found that reducing groups were rapidly liberated from amylopectin, soluble and insoluble starch compared to amylose and glycogen. B. brevis alpha-amylase acted via endo-attack producing mainly maltopentaose during the first hour of hydrolysis. The enzyme showed high activity towards maltohexaose and maltoheptaose. The alpha-amylase from B. brevis had a neutral pI and was found to be a glycoprotein, containing 9.2% (by mass) neutral sugars. The enzyme protein possessed a unique high glycine content. Calcium or sodium ions in appropriate concentrations were required for enzyme thermostability. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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