Abstract
Protease inhibitors specific for cysteine proteases (oryzacystatin), trypsin, chymotrypsin, and subtilisin in 11 major cultivars of rice grown in California are described. The amount of each inhibitor varied considerably with cultivar and was independent of the amount of the other inhibitors. With the exception of subtilisin inhibitor, each of the inhibitors was mainly in the bran fraction of the rice grain. Substrate polyacrylamide gel electrophoresis showed that these protease inhibitors were different low molecular weight proteins ranging in size from 11.5 to 22.0 kDa. Characterization of these inhibitors showed broad pH stability, thermal stability up to 100 o C, and inhibitory action against heat-activated Arrowtooth flounder protease(s)
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