Improving the Thermostability and Optimal Temperature of a Lipase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Covalent Immobilization

Table 1

Matrix of the experimental design to determine optimal pH and temperature of the immobilized lipase from Pyrococcus  furiosus. Coded and real (in parenthesis) variables and experimental values of enzyme activity for the different experimental conditions.

Assay	pH	Temperature (°C)	Octyl agarose activity (U/g of support)	Glyoxyl agarose activity (U/g of support)
1	−1 (6)	−1 (50)	135.13	117.90
2	0 (7)	−1 (50)	217.30	162.09
3	1 (8)	−1 (50)	190.30	123.68
4	−1 (6)	0 (70)	0	169.60
5	0 (7)	0 (70)	312.05	352.92
6	0 (7)	0 (70)	297.10	352.20
7	0 (7)	0 (70)	244.91	324.40
8	0 (7)	0 (70)	277.44	348.73
9	0 (7)	0 (70)	316.53	—
10	1 (8)	0 (70)	114.70	186.07
11	−1 (6)	1 (90)	0	191.70
12	0 (7)	1 (90)	0	480.85
13	1 (8)	1 (90)	0	213.43