Biochemistry

milk. Lipase activators are bile salts, especially taurocholate. In milk, lipase promotes the formation of flavoring substances, and lipase of wheat and other cereals contributes to the deterioration of flour. Microbial lipase preparations arc used for hydrolysis of fats in cases where saponification is necessary while preserving biologically active fat-soluble substances (for example, tocopherol). Pectinesterase catalyzes the cleavage of pectin to form methanol andpectate. The enzyme is activated by Na + and Ca 2+ ions. Pectesterase has a high substrate specificity, hydrolyzing almost exclusively methyl groups of pectin compounds. It is an important component of enzyme preparations, which are used to lighten fruit and grape juices, as well as to obtain low molecular weight pectins used in the manufacture of jelly. This enzyme, along with other enzymes, plays an important role in ripening fruits and berries, drying flax, hemp, and fermenting tea and tobacco. Glycosidases catalyze the cleavage of oligosaccharides and glycosides . They catalyze the hydrolysis and transglycosidation, which plays an important role in the synthesis of polysaccharides in plants. Obtained under industrial conditions from sprouted barley. They are divided into several types. The specificity of these types is determined by the size of the helicon ring, the configuration of OH groups in the ring, and the configuration of the glycosidic hydroxyl. These include: a-D- glycosidase, P-D-glycosidase, a-D-galactosidasc, and others. A-D-glycosidase does not have industrial significance. P-D-glycosidase helps to remove bitterness from citrus juices, and also helps to release flavoring components from P- glycosides. Glycans differ from glycosidases in the longer chain length of the substrates on which they act. The following vigorous glycanases are distinguished on the basis of substrate specificity: a-amylase (substrate — starch, dextrins); fl-amylase (substrate - starch, dextrins); glucoamylase (substrate - starch, dextrins, maltose); inulase (substrate - inulin); polygalacturonase (substrate - pectin, polygalacturonic acid). a-amylase cleaves the a- 1,4 bond in polysaccharides containing three or more glucose residues. It is found in saliva, pancreatic juice, in sprouted grains, in molds and bacteria. For the manifestation of maximum enzyme activity, the presence of the Ca 2+ cofactor is necessary. This enzyme contributes to a rapid decrease in the viscosity of starch paste, so it is called diluting or dextrinogenous amylase. Used in the preparation of starch syrup, wort and mash. fl-amylase catalyzes the degradation of starch to form maltose and dextrins. Since P-amylase releases maltose from amylase and amylopectin, it is called saccharified amylase or sugar amylase. Contained in higher plants. Sources of the enzyme are barley, rye, wheat, soybeans, and beans. Used in the production of wort and mash, starch syrup and as a baking improver. In addition, syrups used in 98