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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