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Affinity chromatography of mustard beta-amylase on starch columns.

An affinity chromatography method for purification of beta-amylase from cotyledons of white mustard seedlings (Sinapis alba L.) is described. beta-Amylase is bound to starch column, while other contaminating proteins are eluted with the binding buffer. The bound beta-amylase is eluted by including dextrin (1%, w/v) in binding buffer. This method yielded a homogeneous preparation of beta-amylase enzyme, which migrated as a single polypeptide band in SDS gel electrophoresis.