Analyses of thermal stability of the wild-type and the mutants of Erv-C.

<p>A. Determination of optimum temperature of activity (<i>T</i>_opt) of the wild-type and the mutants of Erv-C. Purified pro-enzymes (10–20 µg) were converted to their respective mature forms and the percentage residual enzyme activities were determined with respect to the maximum activity using an azocasein assay at different temperatures as described in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0062619#s2" target="_blank">Materials and methods</a>. <b>B.</b> Effect of temperature on activity of the wild type and the mutants of Erv-C. Each purified pro-enzyme (10–20 µg) was treated for 10 min at different temperatures followed by activation of the pro-enzymes to their respective mature forms. The percentage residual enzyme activities (at each temperature) were determined with respect to the maximum activity using an azocasein assay. Each data point is an average of three independent experiments having similar values for both the graphs.