1. Figure 1.- Effect of detergent on the activity of Lecitase lipase against p-NPB.
Experimental condictions are describeb in methods. Relative activity consideres
100 the lipase activity in absence of detergent. Circles: Triton X-100, squares: CTAB.

2. Aquí falta el blanco, en la leyenda pones que los
circulos es el blanco y me imagino que es la suspension
Figure 2.- Immobilization course of Lecitase lipase on octyl-agarose support.
Supernatant of the immobilization suspension (triangles),supernatant of the blank suspension (circles).
The experiments were performed as described in materials and methods.

3. Figure 3.- Desorption of Lecitase lipase adsorbed on octyl-agarose by progressive
addition of CTAB. Experiments were performed at 25 ◦C and pH 7.

4. Tabla o cursos de inmovilizacion en PEI y BRCN

5. Figura 5. - Thermostability of the differents preparation of lecitase
Figura 5.- Thermostability of the differents preparation of lecitase. Inactivation was carried out
in 25 mM sodium phosphate buffer, pH 7 and 45ºC. Squares:BrCN-lecitase;
triangles: Octyl-lecitase; circles: PEI-lecitase.

6. Figure 4.- Effect of the CTAB concentration on the activity againts p-NPB of differnets
immobilized preparations of Lecitase. Relative activity considers 100 the lipase activity in
absence of detergent. Rhombus: BrCN-lecitase, squares: PEI-lecitase.

7. Figure 6. - Thermostability of the lecitase
Figure 6.- Thermostability of the lecitase. Inactivation was carried out in 25 mM sodium
Phosphate buffer, pH 5 and 55ºC. Squares:Lecitase soluble; triangles: PEI-Lecitase.

8. INACTIVACION DE DERIVADOS DE LECITASE
EN PRESENCIA DE 30% DE DISOLVENTES A 25ºC Y pH 7

9. Figure 7. - Thermostability of the differents preparation of lecitase
Figure 7.- Thermostability of the differents preparation of lecitase. Inactivation was carried out
in 25 mM sodium phosphate buffer, pH 5 and 45ºC. Squares:BrCN-lecitase;
triangles: PEI-lecitase; circles: Soluble lecitse; rhombus: Octyl-lecitase.

10. Table 1. Hydrolytic resolution of (±)-Hydroxy-phenylacetic acid methyl ester catalyzed by Lecitase immobilized at 25°C and different pH.
Deivate
Condictions
Act. ee E
Isomer
OCTYL
pH 5
0.018
0.52
3.35 R
pH 7
0.083
0.46
3.02
PEI
0.033
0.75
7.47
0.058
0.51
3.34
0.01%CTAB
2.91
BrCN
0.001
0.37
2.21
0.0016
0.69
5.74
0.0017
0.61
4.35
Ee=enantiomeric excess of the product at 15% of conversion; E=value of enantioselectivity.

11. Derivate Condictions Act. ee E Isomer OCTYL pH 5 0.0023 0.99 >100 R
Table 2. Enantioselectivity of immobilized preparations of Lecitase-catalyzed hydrolysis of 2-O-butyryl-2-phenylacetic acid at different condictions.
Derivate
Condictions
Act. ee E
Isomer
OCTYL
pH 5
0.0023
0.99
>100 R
pH 7
0.0018*
0.84 12
PEI
0.0011
0.75 8
0.0004*
0.29 2
0.01%CTAB
BrCN
0.0005
0.92 26 S
0.0014*
0.13
1.3
* Actividad medida en UI / hora , el resto son actividades por minuto.
Ee=enantiomeric excess of the product at 15% of conversion; E=value of enantioselectivity.