Catalytic and thermodynamic properties of an acidic α-amylase produced by the fungus ATHUM 8891.

An extracellular acid stable α-amylase from ATHUM 8891 (PV8891 α-amylase) was purified to homogeneity applying ammonium sulfate fractionation, ion exchange and gel filtration chromatography and exhibited a reduced molecular weight of 75 kDa. The purified enzyme was optimally active at pH 5.0 and 60 °C and stable in acidic pH (3.