Copper, zinc superoxide dismutase from Caragana jubata: A thermostable enzyme that functions under a broad pH and temperature window
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- 作者：Arun Kumara ; 1 ; Meetal Sharmaa ; Pardeep Kumar Bhardwaja ; 2 ; Surender Kumar Vatsa ; b ; Dharam Singha ; b ; Sanjay Kumara ; b ; sanjaykumar@ihbt.res.in" class="auth_mail" title="E-mail the corresponding author ; director@ihbt.res.in" class="auth_mail" title="E-mail the corresponding author
- 关键词：Reactive oxygen species ; Superoxide dismutase ; Autoclavability ; Thermostability ; Thermal inactivation ; Kinetic stability ; Oligomers ; CD spectroscopy
- 刊名：Process Biochemistry
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：51
- 期：10
- 页码：1434-1444
- 全文大小：1818 K
文摘
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A highly thermostable Cu, Zn superoxide dismutase (SOD) was cloned and characterized from Caragana jubata.
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This enzyme tolerated autoclaving and operated under a broad window of temperature and pH.
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The half-time of thermal inactivation for Cj-Cu, Zn SOD was 95 ± 21min.
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Resistance to sodium dodecyl sulfate (SDS) binding, urea, and heat denaturation suggested its kinetic stability.
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Further analysis of 94 phylogenetically diverse plants revealed the presence of autoclavable SOD in 15 species.