Biochemical Characterisation of a Glucoamylase from Aspergillus niger Produced by Solid-State Fermentation

In this work, glucoamylase was produced by Aspergillus niger in solid-state fermentation. The enzyme was partially purified by ammonium sulphate precipitation and ion exchange and gel filtration chromatographies. Its molecular mass was estimated as 118.17 kDa by electrophoresis. The partially purified enzyme had an optimum pH range of 4.5-5.0 and an optimum temperature of 60 degrees C, with average activity 152.85 U mL(-1). Thermal and pH stability assays with the crude extract showed that more than 60 % of the activity remained at pH 4.6 and 60 degrees C, even after an exposition to these conditions longer than 24 h. Yet, after purification, the enzyme was stable at these for at least 4 h, which indicated that its purification for use in starch saccharification was inadvisable. K-M and V-max were 0.34 mg mL(-1) and 160.22 U mL(-1), respectively.