Purification and chemical characterization of thermostable amylases produced by Bacillus stearothermophilus
โ Scribed by R.A.K. Srivastava
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 729 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0141-0229
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๐ SIMILAR VOLUMES
The reduced methylviolegen-nitrate reductase of the obligate thermophile, Bacillus stearothermophilus NCA strain 2 I84 (ATCC 120 16), has been purified to electrophoretic homogeneity, 53-fold with a yield of 12.5%. The purification procedure involved solubilization with octyl glucoside, ammonium sul
10 min. The enzyme released fructose exo-wise from the non-reducing end of inulin (M r = 4,5000). The Michaelis constant, catalytic center activity, and specificity constant for inulin at 60 ยฐC and pH 5.0 were 80 mM (360 mg/mL), 460 s -1 , and 5.8 s -1 mM -1 , respectively. The ratio of specificity