| Autor: |
Herrera MDG; Instituto de Química Básica y Aplicada del Nordeste Argentino- IQUIBA NEA (UNNE-CONICET), Facultad de Ciencias Exactas Naturales y Agrimensura, Universidad Nacional del Nordeste, Avenida Libertad 5470, (3400), Corrientes, Argentina.; Cátedra de Fruticultura, Departamento de Producción Vegetal, Facultad de Ciencias Agrarias, Universidad Nacional del Nordeste, Argentina. Sargento J.B. Cabral 2131, (3400), Corrientes, Argentina., Luaces PA; Cátedra de Fruticultura, Departamento de Producción Vegetal, Facultad de Ciencias Agrarias, Universidad Nacional del Nordeste, Argentina. Sargento J.B. Cabral 2131, (3400), Corrientes, Argentina., Liggieri C; Centro de Investigación de Proteínas Vegetales (CIProVe), Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de la Plata, 47 y 115s/N, B1900AVW La Plata, Buenos Aires, Argentina., Bruno M; Centro de Investigación de Proteínas Vegetales (CIProVe), Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de la Plata, 47 y 115s/N, B1900AVW La Plata, Buenos Aires, Argentina., Avanza MV; Instituto de Química Básica y Aplicada del Nordeste Argentino- IQUIBA NEA (UNNE-CONICET), Facultad de Ciencias Exactas Naturales y Agrimensura, Universidad Nacional del Nordeste, Avenida Libertad 5470, (3400), Corrientes, Argentina. |
| Abstrakt: |
Bromelia serra leaves collected from Corrientes, Argentina, were assessed to analyze and characterize the proteolytic system and to evaluate its potential use as an industrial catalyst. The specific activity of the enzymatic extract (EE), which was prepared using acetone as a precipitating agent of the crude extract (CE), increased 2-3 folds with different substrates (hemoglobin, azocasein and casein). The proteins present in the EE have isoelectric points between 4.55-8.15 and they were significant inhibited by pepstatin A (50%) and E-64 (15%). Proteolytic activity in EE presented high activity in acidic pH (2.7-4), and low activity in neutral alkaline pH (6-11.75). The EE optimum activity was reached at 60ºC, and referring to the thermal stability, it retained over 97% of the proteolytic activity after incubation at a temperature range of 37‒60 ºC for 60 min. The effect of reducing agents and ionic strength were also measured, and it showed that the EE had its maximum activity with 5mM of cysteine, and it was inactivated with 2.5 M of NaCl. The chromatography procedures presented two purified enzymes of 21 and 54 KDa with proteolytic activity. The characteristics of the EE suggest that it is a potential candidate as an industrial catalyst. |
