التفاصيل البيبلوغرافية
| العنوان: |
Stability characteristics of a calcium-independent alkaline protease from Nesterenkonia sp. |
| المؤلفون: |
Bakhtiar, Shahrzad1, Andersson, Maria M.1, Gessesse, Amare, Mattiasson, Bo1, Hatti-Kaul, Rajni rajni.hatti-kaul@biotek.lu.se |
| المصدر: |
Enzyme & Microbial Technology. Apr2003, Vol. 32 Issue 5, p525. 7p. |
| مصطلحات موضوعية: |
*PROTEOLYTIC enzymes, *THERMODYNAMICS |
| مستخلص: |
Thermodynamic stability of an alkaline protease from a new alkaliphilic Nesterenkonia sp. AL-20, was investigated and compared with that of Subtilisin Carlsberg. The amount of calcium bound to the AL-20 protease was determined to be only about 0.14 mol/mol of protease. Differential scanning calorimetry scan of the enzyme at increasing temperature showed the denaturation of the enzyme to be a two-state process with melting temperature, Tm of about 74 °C at pH 10.0, which was unaltered upon addition of calcium as well as after treatment with chelating agents. The thermodynamic parameters were nearly the same over a pH range of 7.0–10.0. Tm was reduced to 69.7 °C at pH 6.0 and 72 °C at pH 11.0. The secondary structure of the protease was unaffected during storage at 50 °C, even in the presence of 1% SDS as observed by circular dichroism. The protease activity was extremely stable in the presence of hydrogen peroxide and various sequestering agents used in detergents. [Copyright &y& Elsevier] |
| قاعدة البيانات: |
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