PARTIAL CHARACTERIZATION OF A PEPSIN INHIBITOR FROM SOFT WHEAT BRAN

A protein inhibitor of pepsin was extracted from soft wheat bran and a preliminary characterization was made. It has a high resistance to bo iling and pH extremes (0.8-12). The inhibitor differs in its effective ness against various proteinases: it is active against pepsin and inac tive against cathepsin D, rennin, trypsin, chymotrypsin, and papain. V arious salts interfere with the inhibition of pepsin, and sulfate show s the maximal effect, These properties appear to be considerably diffe rent from those of another aspartic proteinase inhibitor specific agai nst cathepsin D and isolated from potatoes. The wheat proteinase inhib itor might affect food digestion.