Raw starch adsorption-desorption purification of a thermostable beta-amylase from Clostridium thermosulfurogenes.

The beta-amylase from Clostridium thermosulfurogenes was readily adsorbed onto raw starch. The adsorbed beta-amylase was eluted from raw starch by using boiled soluble starch solution as an elutant. The soluble starch treated beta-amylase could not adsorb onto raw starch which indicates that the soluble and insoluble substrate binding sites of the beta-amylase may be the same. The beta-amylase was purified to homogeneity by raw starch adsorption-desorption techniques and octyl-Sepharose chromatography. It had a specific activity of 4188 units/mg protein. The insoluble substrate adsorption-desorption technique may be used for the purification of other enzymes.