Two friabilin components, puroindoline a and GSP-1 were expressed in Escherichia coli. Starch
binding properties of the recombinant polypeptides and of friabilin extracted from wheat flour were
compared in vitro. The produced proteins as well as native wheat friabilin bound to starch granules
prepared from different (soft, hard and durum) wheat cultivars. Starch granules also bound
specifically several wheat endosperm proteins other than friabilin