O. V. Gudzenko¹*, N. V. Borzova¹, L. D. Varbanets¹,
I. I. Seifullina², O. A. Chebanenko², E. E. Martsinko²

¹Zabolotny Institute of Microbiology and Virology, National Academy of Sciences of Ukraine, Kyiv;
²Odessa National University I.I. Mechnikov, Ukraine;
*e-mail: ov_gudzenko@bigmir.net

Received: 11 March 2021; Accepted: 22 September 2021

One of the ways to create new biologically active substances based on enzymes is to obtain highly efficient protein-complex structures. Studies in recent years have shown that the coordination compounds of “essential” germanium with biologically active hydroxycarboxylic and, in particular, with xylaric, acids are characterized by low toxicity and a wide range of pharmacological action. In addition, many of them have proven to be activators of various enzymes. In this regard, the aim of work was to study the effects of mixed ligand and heterometallic coordination compounds of germanium with xylaric acid on the catalytic and some physicochemical properties of Penicillium restrictum IMV F-100139 α-galactosidase and α-L-rhamnosidase. α-Galactosidase activity was determined using p-nitrophenyl-α-D-galactopyranoside as a substrate. The activity of α-L-rhamnosidase was determined using the Davis method. As modifiers of enzyme activity different-ligand and different-metalxylaratogermanates have been used. It was shown that the coordination compound (7) tris(bipyridine)nickel(II) μ-dihydroxyxylaratogermanate(IV) ([Ni(bipy)₃]₂[(OH)₂Ge₂(μ-HXylar)₄Ge₂(μ-OH)₂]∙20Н₂О∙2C₂H₅OH) exerted a significant effect on the catalytic properties of α-L-rhamnosidase and α-galactosidase from P. restrictum. The activation and thermal stabilization of P. restrictum α-L-rhamnosidase in the presence of (7) is based on the combination of all constituents of the effector molecule: cation [Ni(bipy)₃]²⁺ and anion [(OH)₂Ge₂(μ-HXylar)₄Ge₂(μ-OH)₂]^4- metal complex, as well as the location of aromatic amino acids in the enzyme molecule. Weak non-covalent bonds between P. restrictum α-L-rhamnosidase molecules and compound (7) appear to create the conformation that is most favorable for the convergence of the active sites of the enzyme with the substrate.