A highly stable Cu/Zn superoxide dismutase from Withania somnifera plant: gene cloning, expression and characterization of the recombinant protein

Madanala, Raju ; Gupta, Vijayta ; Deeba, Farah ; Upadhyay, Santosh Kumar ; Pandey, Vivek ; Singh, Pradhyumna Kumar ; Tuli, Rakesh (2011) A highly stable Cu/Zn superoxide dismutase from Withania somnifera plant: gene cloning, expression and characterization of the recombinant protein Biotechnology Letters, 33 (10). pp. 2057-2063. ISSN 0141-5492

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Official URL: http://www.springerlink.com/content/e740346084x147...

Related URL: http://dx.doi.org/10.1007/s10529-011-0670-0

Abstract

A gene from Withania somnifera (winter cherry), encoding a highly stable chloroplastic Cu/Zn superoxide dismutase (SOD), was cloned and expressed in Escherichia coli. The recombinant enzyme (specific activity of ~4,200 U mg-1) was purified and characterized. It retained ~90 and ~70% residual activities after 1 h at 80 and 95°C, respectively. At 95°C, thermal inactivation rate constant (K d) of the enzyme was 2.46 × 10-3 min-1 and half-life of heat inactivation was 4.68 h. The enzyme was stable against a broad pH range (2.5-11.0). It also showed a high degree of resistance to detergent, ethanol and protease digestion. This recombinant Cu/Zn SOD could therefore have useful applications.

Item Type:Article
Source:Copyright of this article belongs to Springer.
Keywords:Cu/Zn Superoxide Dismutase; Superoxide Dismutase; Thermostable Enzyme; Winter Cherry; Withania somnifera L.
ID Code:54628
Deposited On:12 Aug 2011 07:06
Last Modified:20 Jun 2012 04:55

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