PROIMI   05436
PLANTA PILOTO DE PROCESOS INDUSTRIALES MICROBIOLOGICOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Partial characterization of esterases and lipases from A. niger MYA 135
Autor/es:
ROMERO, CINTIA MARIANA; PERA, LICIA MARÍA; BAIGORI, MARIO DOMINGO
Lugar:
Tafí del Valle , Tucumán, Argentina
Reunión:
Jornada; XXIII Annual Scientific Meeting; 2007
Institución organizadora:
Tucumán Biology Society
Resumen:
Introduction: Esterases (EC 3.1.1.1) and lipases (EC 3.1.1.3) catalyze hydrolysis and synthesis of esters. Their applications include hydrolysis of fats and oils, resolution of racemic mixtures, etc. Objective: The aim of this work was to study the effects of different conditions on the stability of esterases and lipases from Aspergillus niger MYA 135. Materials and methods: Culture supernatant was preincubated at several pH values and temperatures. Residual activities were analyzed by nPAGE using either á-naphtyl acetate or á-naphtyl mirystate as substrates. Activities already separated by nPAGE were also used to evaluate their stabilities in organic solvents. Results and conclusions: Enzymes were active within the pH and the temperature range tested. Except at pH 9 and at 55°C where some bands were not detected. Enzymes preincubated in either 2-propanol, 2,3-butanodiol or acetone showing the same pattern that the control without incubation. Some bands were not detected after preincubation with propanol, n-hexane, hexanol or n-heptane. No band was observed after preincubation with butanol. One of the bands shows a good stability pattern which justifies its application in biocatalysis. This work was supported by grants PIP 6203 and PICTO 761.