Catalytic properties of mycelium-bound lipases from Aspergillus niger MYA 135.
A constitutive level of a mycelium-bound lipolytic activity from Aspergillus niger MYA 135 was strongly increased 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 degrees 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 degrees C in ethanol. A simple methodology to evaluate suitable transesterification activities in organic solvents was also reported.
Romero
Cintia M
CM
Planta Piloto de Procesos Industriales Microbiológicos (PROIMI), Av. Belgrano y Pasaje Caseros, 4000, Tucumán, Argentina.
Baigori
Mario D
MD
Pera
Licia M
LM
D000438:Alcohols / Q000378:metabolism; D001234:Aspergillus niger / Q000201:enzymology*; D002384:Catalysis; D004795:Enzyme Stability; D005285:Fermentation; D006863:Hydrogen-Ion Concentration; D007218:Industrial Microbiology / Q000379:methods*; D008049:Lipase / Q000378:metabolism*; D025282:Mycelium / Q000201:enzymology; D000069463:Olive Oil; D010938:Plant Oils / Q000494:pharmacology; D012997:Solvents; D013696:Temperature
D000438:Alcohols; D000069463:Olive Oil; D010938:Plant Oils; D012997:Solvents; D008049:Lipase