The achievements of modern enzymology have greatly expanded the possibilities of practical use of enzymes, primarily in medicine and the food industry, which is due to their advantages over chemical catalysts: selectivity and stereospecificity of action, the possibility of achieving high rates of conversion of substrates under relatively mild technological conditions, harmlessness to the environment and humans. The microbial producers have proven themselves as a convenient and economical source of biotechnologically important enzyme preparations of hydrolytic action. One of such enzymes is α-galactosidase, which has the ability to cleave terminal α-linked galactosyl residues from a wide range of natural and synthetic compounds. The review presents data on the spread of the enzyme among different groups of microorganisms and provides a comparative description of their catalytic properties. A range of issues related to the physiological role of the enzyme in plant and animal organisms, localization and functional properties in bacteria and fungi are outlined. The place of α-galactosidase of microorganisms in the modern hierarchical classification of glycosidases is shown. The areas of possible use of the enzyme as an efficient tool for the modification of oligo- and polysaccharides in various industries are described.
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