Abstract
The grains of cereal are able to synthesize and store various protein inhibitors of proteases and amylases. Despite some scientific breakthroughs, there is insufficient information about α-amylase/subtilysin protein inhibitor of wheat grains. Furthermore, when baking bread from germinated wheat grains, the excess activity of α-amylase, which contributed to the restoration of its quality, is suppressed by an inhibitor added from the outside. In our work, the localization of the α-amylase protein inhibitor (PI) in the endosperm and peripheral parts of the grain (shell, aleurone) was determined. In the endosperm, the protein may be free or associated with starch granules. No inhibitor detected in the germ of grain. PI inhibits the catalytic center of Amy1α-amylase of wheat grain, having little influence on the center responsible for the binding of the enzyme to starch granules. The activity and composition of α-amylase in nine samples of wheat meal with high autolytic activity were analyzed (the number of falls is from 248 to 72). FN 91 sec grist showed the most heterogeneous spectrum to the effect of mixtures of wheat’s inhibitor and raw extract from grain bran that were taken from the previous studies on α-amylase enzyme. The results of the experiment showed that exposure to the addition of two drugs of purified and raw inhibitors to grist extract with a low number of drops led to a decrease in the activity of α-amylase (Amy1). The novelty of the work was found to inhibit the localization of protein inhibitors and the catalytic center of wheat α-amylase.