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Stability characteristics of a calcium-independent alkaline protease from Nesterenkonia sp.

Bakhtiar, Shahrzad LU ; Andersson, Maria LU ; Gessesse, Amare; Mattiasson, Bo LU and Hatti-Kaul, Rajni LU (2003) In Enzyme and Microbial Technology 32(5). p.525-531
Abstract
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... (More)
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. (Less)
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organization
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Contribution to journal
publication status
published
subject
keywords
Stability, Nesterenkonia sp., Circular dichroism, Differential scanning calorimetry, Calcium-independent alkaline protease
in
Enzyme and Microbial Technology
volume
32
issue
5
pages
525 - 531
publisher
Elsevier
external identifiers
  • wos:000181908500004
  • scopus:0037426299
ISSN
0141-0229
DOI
10.1016/S0141-0229(02)00336-8
language
English
LU publication?
yes
id
6ddd0d16-5bc4-40a0-aacf-d364fd8cb7e1 (old id 129071)
date added to LUP
2007-06-29 16:02:57
date last changed
2018-01-07 06:09:10
@article{6ddd0d16-5bc4-40a0-aacf-d364fd8cb7e1,
  abstract     = {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.},
  author       = {Bakhtiar, Shahrzad and Andersson, Maria and Gessesse, Amare and Mattiasson, Bo and Hatti-Kaul, Rajni},
  issn         = {0141-0229},
  keyword      = {Stability,Nesterenkonia sp.,Circular dichroism,Differential scanning calorimetry,Calcium-independent alkaline protease},
  language     = {eng},
  number       = {5},
  pages        = {525--531},
  publisher    = {Elsevier},
  series       = {Enzyme and Microbial Technology},
  title        = {Stability characteristics of a calcium-independent alkaline protease from Nesterenkonia sp.},
  url          = {http://dx.doi.org/10.1016/S0141-0229(02)00336-8},
  volume       = {32},
  year         = {2003},
}