α-Amylase from mung beans (Vigna radiata) - Correlation of biochemical properties and tertiary structure by homology modelling

α-Amylase from mung beans was purified to homogeneity by affinity chromatography. Purification was 600-fold and final specific activity achieved was 437 U/mg. Homology modelling studies with mung bean α-amylase were performed using barley α-amylases Amy 1 and Amy 2 as templates. The model showed a very similar structure as expected from the high sequence identity, except the absence of sugar and raw starch binding sites.