Figure 6
From: The allosteric modulation of lipases and its possible biological relevance
Progress of the reaction carried out at low temperature; a, c, e: Amount of compounds 3, 4 and 5 (n [%]); b, d, f: Enantiomeric excess of (S)-4 (% ee); a, b: Transformation catalyzed by lipase from B. cepacia at -40°C; c, d: Transformation catalyzed by lipase from M. miehei at -10°C; e, f: Simulation of the reaction using a constant lipase activity a = 0.004 [14]; The rate constants k1 to k8 are defined in Figure 3; k1 = 35, k2 = 1, k3 = 4, k4 = 140, k5 = 35·10-6, k6 = 1·10-6, k7 = 4·10-6, k8 = 140·10-6.