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.
Subbaramaiah
K
K
Sharma
R
R
D000681:Amylases / Q000032:analysis*; D002846:Chromatography, Affinity / Q000379:methods; D010944:Plants / Q000032:analysis*; D013213:Starch; D001614:beta-Amylase / Q000032:analysis*
D013213:Starch; D000681:Amylases; D001614:beta-Amylase