Catalytic properties of mycelium-bound lipases from Aspergillus MYA 135

CINTIA M. ROMERO & MARIO D. BAIGORI & LICIA M. PERA

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

Springer

Año: 2007 vol. 76 p. 861 - 866

0175-7598

A constitutive level of a mycelium-bound lipolytic activity from Aspergillus niger MYA 135 was stronglyincreased by 97% in medium supplemented with 2% olive oil. The constitutive lipase showed an optimal activity in the pH range of 3.0?6.5, while the mycelium-bound lipase activity produced in the presence of olive oil had two pH optima at pH 4 and 7. Interestingly, both lipolytic sources were cold-active showing high catalytic activities in the temperature range of 4?8°C. These mycelium-bound lipase activities were also very stable in reaction mixtures containing methanol and ethanol. In fact, the constitutive lipase maintained almost 100% of its activity after exposure by 1 h at 37°C in ethanol. A simple methodology to evaluate suitable transesterification activities in organic solvents was also reported.