Preparation and Catalytic Properties of Immobilized Thermoalkaliphilic T1 Lipase from Geobacillus sp. Strain T1
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Abstract:
Using glucan as carrier, thermoalkaliphilic T1 lipase from Geobacillus sp. strain T1 was immobilized via covalent binding. The optimized conditions for enzyme preparation were established and catalytic properties of the immobilized T1 lipase were determined. In a single-factor experiment, specific activity of immobilized T1 lipase reached 50.25 U/mg matrix by using optimal conditions including 1.23% 2-iodoxy benzoate, immobilization temperature of 50 ℃ and time for 2 h. Immobilized T1 lipase was used to catalyze the alcoholysis of olive oil and methanol, yielding 14.08% fatty acid methyl esters after 60 h. Meanwhile, the thermostability and organic solvent tolerance of the immobilized T1 lipase were also studied. The results indicated that the immobilized T1 lipase could maintain more than 70% of its activity after a 7-h incubation at 60 ℃, and the activity increased to 120% to 140% after treatment with n-butanol, n-propanol, and isopropanol, in addition to methanol and ethanol. These results demonstrate that immobilized T1 lipase has a potential to catalyze the reaction involving methanol to produce biodiesel and exhibits good thermostability and organic solvent tolerance; therefore, it has potential for industrial application.
