Catalytic properties of purified alpha amylase from Aspergillus flavus cultivated on low-cost agricultural substrate

dc.creatorOlushola E Owolabi
dc.creatorOladipo O Olaniyi
dc.creatorFelix A Akinyosoye
dc.date2023
dc.date.accessioned2026-07-07T03:30:36Z
dc.descriptionAspergillus 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.
dc.formatapplication/pdf
dc.identifier0304-2847
dc.identifierhttps://www.redalyc.org/articulo.oa?id=179975180010
dc.identifierhttps://www.redalyc.org/journal/1799/179975180010/
dc.identifierhttps://www.redalyc.org/journal/1799/179975180010/html/
dc.identifierhttps://www.redalyc.org/journal/1799/179975180010/179975180010.epub
dc.identifierhttps://www.redalyc.org/journal/1799/179975180010/movil
dc.identifier10.15446/rfnam.v76n1.100842
dc.identifier.urihttp://hdl.handle.net/123456789/435866
dc.languageen
dc.publisherUniversidad Nacional de Colombia
dc.relationhttp://www.redalyc.org/revista.oa?id=1799
dc.rightsRevista Facultad Nacional de Agronomía - Medellín
dc.sourceRevista Facultad Nacional de Agronomía - Medellín (Colombia) Num.1 Vol.76
dc.subjectAgrociencias
dc.titleCatalytic properties of purified alpha amylase from Aspergillus flavus cultivated on low-cost agricultural substrate
dc.typeartículo científico

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