IQUIBA-NEA   25617
INSTITUTO DE QUIMICA BASICA Y APLICADA DEL NORDESTE ARGENTINO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
CHARACTERIZATION OF ALKALINE AND ACIDIC PROTEOLYTIC ENZYMES FROM PALOMETA (Pygocentrus nattereri) VISCERA
Autor/es:
ACEVEDO GÓMEZ, ANTONELLA; MEDINA, DAIANA; GÓMEZ, GABRIELA; LEIVA, LAURA C.
Lugar:
Buenos Aires
Reunión:
Jornada; XX Jornadas anuales de la Sociedad Argentina de Biología; 2018
Institución organizadora:
Sociedad Argentina de Biología
Resumen:
Fish viscera are regarded as a source of enzymes (proteases) whit high commercial value and many industrial and scientific applications. Palometa (Pygocentrus nattereri) is widely distributed throughout Paraná River and its proteases were not study until the present. The objective of this work was to study the enzymatic activity and stability of trypsin and pepsin enriched extracts obtained from pyloric caeca and gastric mucosa tissues. Samples were provided from local farmers. Preparations of extracts were made by mechanical and sonic digestion of tissues whit the addition of appropriates buffers (1:5 tissue/buffer). Trypsin extract (alkaline) proteolytic activity was assayed with using a-Nbenzoyl-DL-arginine-p-nitroanilide (BAPNA) as substrate, while pepsin extract (acid) activity was estimated by acid haemoglobin method. Enzymatic activity and stability were evaluated under different conditions of pH (1-12), temperature (0-80ºC). Alkaline extract exhibited the highest activity at 50-60 ºC-pH 11-12, showed pH stability between 2 and 12 and remained thermostable until 60°C. Acid extract showed its optimum activity at pH 1-2, and 45°C, was stable at a pH range of 1-6 and at temperatures below 45°C. This information will be primordial for ulterior purification process of trypsin and pepsin and the obtainment of a high quality enzymes. These extracts present attractive enzymatic properties, so they could be used for industrial applications, such as additive for detergent laundry and collagen extraction for alkaline and acid extract, respectively.