5-56: Production and preliminary characterization of a lipase from thermophilic Myceliophthora sp F2.1.4

Utilization of lipases as catalysts for biodiesel production has a great potential compared to chemical methods. This study aimed to evaluate lipase production by the thermophilic fungi Myceliophthora sp F2.1.4, using solid-state (SSF) and submerged (SmF). For SSF it was used the culture medium composed by (w/w %) 5 peptone, 0.5 K₂HPO₄, 0.12 MgSO₄, 62.3 sugar cane bagasse, 21.4 olive oil, 5.2 sucrose, 2.6 NH₄NO₃ and 2.5 mL water/g of solid material, 5x10⁶ spores for inoculum. The enzyme extraction was carried out using a 1% Triton X-100 solution. In these conditions was obtained a crude enzyme solution with 16 U/mL of lipase. Using the same medium without sugar cane bagasse in SmF condition, the it was obtained a crude enzyme solution with 0.20 U/mL. The partial characterization of the lipase indicated the maximum activity at pH 5 to 7 and at 35^oC. The enzyme was stable for two h in temperature from 35 to 50^oC and pH from 4 to 9. The enzyme presented preference to long chain fatty acid proving that it is a true lipase and it was able to catalyses the transesterification reaction. The lipase was tolerant to ethanol and methanol suggesting a potential enzyme to biodiesel production. When it was immobilized in alginate it was possible to reuse for 6 times. These results show that the physicochemical properties of the lipase from Myceliophthora sp F 2.1.4 have a great potential for industrial applications.