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. 1999 Sep;65(9):3969–3975. doi: 10.1128/aem.65.9.3969-3975.1999

FIG. 3.

FIG. 3

Effect of temperature on the activity of the 47-kDa protease. (A) The enzyme (∼2.1 μg) was incubated in 600 μl of Tris buffer containing 5 mM MgCl2 and 1% azocasein for 30 min at various temperatures, and caseinolytic activity was measured as described. The values obtained at 37°C were taken as 100%. Relative activities are the averages for two independent experiments. (B) Arrhenius plot showing thermal deactivation of the 47-kDa protease. The ln of specific activity (k) (100 × EU) was plotted against the reciprocal of absolute temperature (T).