Studies on Thermophilic α-Amylase from Bacillus stearothermophilus
- 1 January 1970
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 67 (1) , 77-82
- https://doi.org/10.1093/oxfordjournals.jbchem.a129236
Abstract
The effects of pH, urea and EDTA on the thermal stability of thermophilic α-amylase [EC 3.2.1.1] were studied by the measurements of enzymatic activity and optical activity in the far ultraviolet region at various temperatures. Thermophilic α-amylase became unstable by removing calcium and protected against an inactivation in the presence of saturation level of calcium. Thermal stability of the enzyme was affected by 10–2M EDTA than 8 M urea. This was more remarkable in thermophilic α-amylase than in B. subtilis α-amylase. These results suggested that calcium ion plays an important role in thermal stability of thermophilic α-amylase molecule. In the presence of 8 M urea, thermophilic α-amylase scarcely showed an alteration on the CD spectrum at room temperature, although the presence of 8 M urea promoted the dena-turation of thermophilic α-amylase at the elevated temperature.Keywords
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