PROIMI   05436
PLANTA PILOTO DE PROCESOS INDUSTRIALES MICROBIOLOGICOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Extracellular and mycelium-bound lipase production by Penicillium corylophilum.
Autor/es:
RODRIGUEZ, EMILIO; ROMERO, CINTIA MARIANA; PERA, LICIA MARÍA; KRIEGER, NADIA; CASTRO, GUILLERMO RAÚL; BAIGORI, MARIO DOMINGO
Lugar:
Tafi del Valle, Tucumán, Argentina.
Reunión:
Jornada; XXII Annual Scientific Meeting.; 2006
Institución organizadora:
Tucumán Biology Society.
Resumen:
EXTRACELLULAR AND MYCELIUM-BOUND LIPASE PRODUCTION BY PENICILLIUM corylophilum   Rodríguez E, Romero C, Pera L, Krieger N, Castro G and Baigorí M   PROIMI Av. Belgrano y Pje. Caseros, 4000 Tucumán. Tel: 4344888, e-mail: baigori@hotmail.com    Introduction. Lipases (EC 3.1.1.3) are enzymes that catalyze the hydrolysis of triglycerides in the oil-water interface. Both extracellular and mycelium-bound lipases from fungi are important in industrial applications. In particular, the use of a naturally-bound lipase can be cost effective because the biomass can be used directly, thus eliminating isolation, purification and immobilization procedures. Objective. The aim of this work was the evaluation of both extracellular and mycelium-bound lipase activity production by a strain of Penicillium corylophilum. Materials and methods. P. corylophilum was grown at 30°C in MB medium with and without supplementation 2% olive oil. MB (g/l): sacarose 10; NH4NO3 2; KH2PO4 1; MgSO4.7H2O 0.2; CuSO4.5H2O 0.06; pH7. Lipase production was monitored using p-nitrophenylpalmitate as substrate. Both extracellular and mycelium-bound specific lipase activity was calculated. Conclusions. Specific lipase activities obtaining in presence of olive oil were 7.6 U per µg of protein (supernatant) and 179.1 U per g of dry weight (mycelia). This work was supported by grant CABBIO 2000 cod 012