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

<div>Surface response and contour lines for lipase immobilized on octyl-agarose (a) and on glyoxyl-agarose (b) as a function of temperature and pH. The enzyme immobilized on Octyl-agarose showed an optimal temperature of 66°C and pH around 7. The enzyme immobilized on glyoxyl agarose reached activities at temperatures as high as 90°C and pH 7.</div>

BioMed Research International

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Figure 2: Improving the Thermostability and Optimal Temperature of a Lipase from the Hyperthermophilic Archaeon <i>Pyrococcus furiosus</i> by Covalent Immobilization 

Figure 2 | Improving the Thermostability and Optimal Temperature of a Lipase from the Hyperthermophilic Archaeon Pyrococcus furiosus by Covalent Immobilization 