Abstract
This study reports a thermostable Cu, Zn superoxide dismutase (SOD) obtained from a high-altitude plant Caragana jubata (Cj-Cu, Zn SOD). The expression of Cj-Cu, Zn SOD in Escherichia coli followed by purification yielded a 17.5kDa protein with a specific activity of 1547±39 units/mg of protein at 0°C. The enzyme (i) functioned across a temperature range of −10 to +80°C with optimum activity at 0–4°C; (ii) performed well in a pH range of 6–9 with optimum activity at pH 7.5; (iii) was resistant to denaturation by sodium dodecyl sulfate (SDS) and urea; and (iv) existed in both monomeric and dimeric forms, the latter being more active. The enzyme exhibited activity upto 80°C (kd=8.00±0.17×10−3min−1, t1/2=95±21min), and tolerated autoclaving (heating at 121°C at a pressure of 1.1kg/cm2 for 20min). Circular dichroic spectroscopy analysis confirmed the thermostable nature of Cj-Cu, Zn SOD. Analysis in 94 phylogenetically diverse plant species across varied habitat preferences revealed the presence of autoclavable SOD in 15 species. SODs with unique properties of thermo/kinetic stability can be exploited for various applications in cosmetic, food, and pharmaceutical industries.
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