Enhanced trypsin thermostability in Pichia pastoris through truncating the flexible region

Table 2 Kinetic parameters of WT and variants

Enzymes	K_m (μM)	k_cat (s⁻¹)	k_cat/K_m (mM⁻¹ s⁻¹)	Specific activity (U/mg)
WT	28.80 ± 2.94	0.634 ± 0.030	22.014 ± 1.45	105,614.2 ± 4154.28
D3	58.60 ± 3.30	0.676 ± 0.007	11.536 ± 0.87	73,850.3 ± 1385.34
D5	33.40 ± 4.11	0.652 ± 0.007	19.521 ± 1.05	102,234.8 ± 5238.41
D7	11.01 ± 0.94	0.604 ± 0.024	54.910 ± 3.56	196,961.5 ± 8182.93
D9	27.04 ± 3.35	0.624 ± 0.099	23.111 ± 2.19	108,760.9 ± 5205.32
D11	7.50 ± 0.29	0.580 ± 0.019	77.330 ± 4.98	340,425.6 ± 9314.77

Each value was calculated from triplicate experiments. Means ± standard deviations
The enzyme activities were measured at 25 °C

ISSN: 1475-2859