Abstract
Two proteases capable of decreasing dough strength when added to wheat flour were purified from Maitake and these were both thought to be peptidyl-Lys metalloendopeptidase. The major purified protease SP-3-A hydrolyzed high-molecular-weight glutenin subunits preferably to the other glutenin subunits. SP-3-A cleaved peptide bonds adjacent to the N-terminal of lysine in the high-molecular-weight glutenin subunit.