Immobilization and Characterization of a Recombinant Thermostable Lipase (Pf2001) from <i>Pyrococcus furiosus</i> on Supports with Different Degrees of Hydrophobicity

<table>Response surface for immobilized enzyme activity on (a) butyl and (b) octadecyl Sepabeads (U<svg height="5.4499998" id="M60" style="vertical-align:-0.0pt" version="1.1" viewbox="0 0 4 5.4499998" width="4" xmlns="http://www.w3.org/2000/svg" xmlns:xlink="http://www.w3.org/1999/xlink">
<g transform="matrix(.017,-0,0,-.017,.062,5.388)"><path d="M170 255q0 -25 -16 -41t-40 -16t-40 16t-16 41t16 41.5t40 16.5t40 -16.5t16 -41.5z" id="x22C5"></path></g>
</svg>g<sup>-1</sup> of support) as a function of temperature and pH. The surfaces were constructed only with the statistically significant variable.</table>

Enzyme Research

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Figure 2

Figure 2: Immobilization and Characterization of a Recombinant Thermostable Lipase (Pf2001) from <i>Pyrococcus furiosus</i> on Supports with Different Degrees of Hydrophobicity 

Figure 2 | Immobilization and Characterization of a Recombinant Thermostable Lipase (Pf2001) from Pyrococcus furiosus on Supports with Different Degrees of Hydrophobicity 