Stability characteristics of a calcium-independent alkaline protease from Nesterenkonia sp.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/129071
- author
- Bakhtiar, Shahrzad LU ; Andersson, Maria LU ; Gessesse, Amare ; Mattiasson, Bo LU and Hatti-Kaul, Rajni LU
- organization
- publishing date
- 2003
- type
- 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
- 2016-04-01 12:23:40
- date last changed
- 2022-03-05 23:00:18
@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}},
keywords = {{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}},
doi = {{10.1016/S0141-0229(02)00336-8}},
volume = {{32}},
year = {{2003}},
}