Fig. 6

Kinetic analysis of LipSm. Merged curves of the dependencies of Michaelis–Menten parameters k_cat/K_m (filled square solid lines) and k_cat (filled triangle dotted lines) versus the pH value, as well as versus the absolute temperature, and an energy diagram: a estimates of parameters k_cat/K_m and k_cat versus the pH value, using 4-nitrophenyl acetate as substrate, where (k_cat/K_m)^lim = 2.33 ± 0.26 M⁻¹ s⁻¹, pK_a1 = 7.42 ± 0.10 and pK_a2 = 8.29 ± 0.10, as well as (k_cat)^lim = 1.33 × 10⁻³ ± 0.03 × 10⁻³, pK_a1 = 7.09 ± 0.03 and pK_a2 = 9.36 ± 0.04; b estimates of parameters k_cat/K_m and k_cat versus the pH value, using 4-nitrophenyl butyrate as substrate, where (k_cat/K_m)^lim = 29.24 ± 0.71 M⁻¹ s⁻¹, pK_a1 = 7.78 ± 0.04 and pK_a2 = 9.93 ± 0.05, as well as (k_cat)^lim = 44.78 × 10⁻³ ± 0.87 × 10⁻³, pK_a1 = 7.52 ± 0.02 and pK_a2 = 10.33 ± 0.60; c the dependencies of parameters k_cat/K_m and k_cat versus the absolute temperature, using 4-nitrophenyl acetate as substrate; d energy diagram of hydrolysis of substrate 4-nitrophenyl acetate by the novel lipase (the value of Arrhenius pre-exponential factor was assumed as 6 × 10¹² s⁻¹)