Catalytic properties of purified alpha amylase from Aspergillus flavus cultivated on low-cost agricultural substrate
Propiedades catalíticas de alfa amilasa purificada de Aspergillus flavus cultivada en sustrato agrícola de bajo costo
DOI:
https://doi.org/10.15446/rfnam.v76n1.100842Keywords:
Alpha amylase, Characterization, Fermented cereals, Organic composite, Purification, Stability (en)Alfa amilasa, Caracterización, Cereales fermentados, Compuestos orgánicos, Purificación, Estabilidad (es)
Aspergillus flavus isolated from fermented millet flour produced a crude enzyme, which was purified via ammonium sulphate precipitation and subsequent chromatographic techniques. The biochemical characteristics of the purified amylase were thereafter investigated showing activity in a wide range of pH and temperature, with optimal conditions of pH 6.0 and 50 °C. The enzyme retained even 89% of its activity after 1 h at 50 °C and 2 h at pH 6.0. The purified enzyme was stimulated by Ca2+, Zn2+ and Co2+, while Hg2+ and EDTA caused mild inhibition of α-amylase activity. The kinetic indices (Km and Vmax) and molecular weight of the enzyme were estimated in 1.71 mg mL-1, 2.133 μmol min-1 mL-1 and 45 kDa respectively. The catalytic properties of α-amylase from A. flavus makes it a promising candidate for use in various starch processing industries.
Aspergillus flavus aislado de harina de mijo fermentada produjo una enzima cruda, que se purificó mediante precipitación con sulfato de amonio y técnicas cromatográficas. Posteriormente se investigaron las características bioquímicas de la amilasa purificada mostrando actividad en un amplio rango de pH y temperatura, con condiciones óptimas de pH 6,0 y 50 °C. La enzima retuvo incluso el 89% de su actividad después de 1 h a 50 °C y 2 h a pH 6,0. La enzima purificada fue estimulada por Ca2+, Zn2+ y Co2+, mientras que Hg2+ y EDTA causaron una leve inhibición de la actividad de la α-amilasa. Los índices cinéticos (Km y Vmax) y peso molecular de la enzima se estimaron en 1,71 mg mL-1, 2,133 μmol min-1 mL-1 y 45 kDa respectivamente. Las propiedades catalíticas de la α-amilasa de A. flavus la convierten en un candidato prometedor para su uso en diversas industrias de procesamiento de almidón.
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