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Table 5 Apparent Vmax and KM average variation after X time exposure at different temperatures

From: Recombinant laccase rPOXA 1B real-time, accelerated and molecular dynamics stability study

     Non-linear, least-squares based regression
Temperaturea Time Number of Vmax ± SD KM ± SD
(°C) (K) (Month) (pool) (mM min−1) (mM)
−32.55 ± 4.12 240.98 ± 5.38 12 27 0.0102 ± 0.0004 0.0414 ± 0.0046
4.32 ± 1.22 277.40 ± 1.32 12 27 0.0104 ± 0.0005 0.0435 ± 0.0057
24.99 ± 0.25 297.53 ± 3.88 6 18 0.0102 ± 0.0004 0.0466 ± 0.0064
30.12 ± 1.11 303.27 ± 1.11 6 18 0.0104 ± 0.0004 0.0477 ± 0.0076
36.43 ± 0.23 309.58 ± 0.23 4 12 0.0094 ± 0.0005 0.1016 ± 0.0736
41.64 ± 0.52 314.79 ± 0.52 1 3 0.0096 ± 0.0006 0.1433 ± 0.1564
  1. aTemperatures at which the samples were stored during the real-time stability study
  2. Kinetic enzymatic reaction conditions were ABTS dissolved in 0.1 M citrate buffer at concentration between 0.1–3 mM, pH 3.0 ± 0.2. An enzyme solution with an activity of 10 UL− 1, reaction temperature 25 °C