Ukr.Biochem.J. 2023; Volume 95, Issue 4, Jul-Aug, pp. 46-54

doi: https://doi.org/10.15407/ubj95.04.046

The influence of coordination compounds with malatogermanate/stannate anions and 1,10-phenanthroline cations of 3D metals on α-L-rhamnosidase activity of Penicillium tardum, Penicillium restrictum and Eupenicillium erubescens

31.08.2023   Uncategorized   No comments

O. V. Gudzenko1*, N. V. Borzova1, L. D. Varbanets1,
I. I. Seifullina2, O. E. Martsinko2, E. V. Afanasenko2

1D.K. Zabolotny Institute of Microbiology and Virology, National Academy of Siences of Ukraine, Kyiv;
2I.I. Mechnikova Odesa National University, Odesa, Ukraine;
*e-mail: alena.gudzenko81@gmail.com

Received: 01 May 2023; Revised: 15 July 2023;
Accepted: 7 September 2023; Available on-line: 12 September 2023

The search for effectors capable of influencing the catalytic activity of enzymes is an important area of modern enzymology. The aim of the study was to investigate the ability of 6 coordination compounds with malatogermanate/stannate anions and 1,10-phenanthroline cations of 3d metals to modify α-L-rhamnosidase activity of Penicillium tardum, Penicillium restrictum and Eupenicillium еrubescens strains. α-L-Rhamnosidase activity was determined by the Davis method using naringin as a substrate. It was demonstrated­ that [Ni(phen)3]2[{Sn(HMal)2(Mal)}Cl]•14H2O) in 0.1% concentration had the most pronounced activating effect on α-L-rhamnosidase activity of all strains studied. Noncompetitive inhibition of α-L-rhamnosidase in E. еrubescens by [Cu(phen)3]2[{Sn(HMal)2(Mal)}Cl]•10H2O was shown. The obtained results expand the idea of glycosidases possible activators and inhibitors and indicate the perspective of their use in modern biotechnological processes.

Keywords: , , , , , , ,

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