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ISSN 2410-7751 (Print)
ISSN 2410-776X (Online)

cover biotech acta general

Biotechnologia Acta Т. 16, No. 4, 2023
P. 5-21, Bibliography 99, Engl.
UDC:  577.151:579.22

Full text: (PDF in English)


N. V. Borzova, L. D. Varbanets

Zabolotny Institute of Microbiology and Virology of the National Academy of Sciences of Ukraine

One of the important problems of current biotechnology is the usage of enzymes of microbial origin for destruction of poorly soluble compounds and synthesis of new drugs. In recent years a great deal of researchers’ attention has been given to such technologically promising carbohydrases as O-glycosylhydrolases catalyzing the hydrolysis of O-glycoside links in glycosides, oligo- and polysaccharides, glycolipids, and other glycoconjugates.

Aim. The review provides data on the position of α-L-rhamnosidases in the modern hierarchical classification of glycosidases and presents data available in the literature on the features of the enzyme structure in various microorganisms.

Methods. The publications from the following databases were analyzed: PubMed (, the Carbohydrate-Active enZYmes (, the BRENDA Enzyme Database (

Results. Data on the physicochemical, catalytic, and kinetic properties of α-L-rhamnosidases in microorganisms of different taxonomic groups have been systematized. The peculiarities of the substrate specificity of the enzyme depending on the nature of the protein and the growing conditions of the producer are characterized.

Conclusions. Functional properties and specificity action of microbial α-L-rhamnosidases suggest their broad-range applicability for food and animal feed processing, as well as obtaining biologically active compounds for the pharmaceutical industry and medicine.

Key words: α-L-rhamnosidase, microorganisms, physicochemical properties, specificity, derhamnosylation, flavonoids

© Palladin Institute of Biochemistry of the National Academy of Sciences of Ukraine, 2023