Characterization of a bifunctional wheat inhibitor of endogenous α‐amylase and subtilisin

Abstract

A bifunctional α‐amylase/serine protease inhibitor which inhibits germination‐specific cereal α‐amylases of the Graminae subfamily Festucoideae as well as bacterial subtilisins has been isolated from wheat grains. This protein has M r ≈20500 and p I ≈7.2. The amino acid composition and N‐teminal sequence (45 residues) show that the inhibitor is homologous with cereal and leguminous inhibitors of the soybean trypsin inhibitor (Kunitz) family.