Tag Archives: Penicillium tardum
Influence of heterometallic Ge(IV) – 3d-metals complexes on microbial rhamnosidase, galactosidase and protease activity
O. V. Gudzenko1*, L. D. Varbanets1, I. I. Seifullina2,
О. E. Martsynko2, O. A. Finik3, K. K. Tsymbaliuk2,3
1Zabolotny Institute of Microbiology and Virology,
National Academy of Sciences of Ukraine, Kyiv;
2Odesa I. I. Mechnikov National University, Ukraine;
3LLC “Inspectorat Ukraine”, Ukraine;
*e-mail: alena.gudzenko81@gmail.com
Received: 18 March 2025; Revised: 12 May 2025;
Accepted: 11 June 2025; Available on-line: 07 July 2025
In recent years, the attention of researchers has been attracted by coordination compounds of germanium with various bioligands, which may be used both as activator or inhibitor of enzymes. The aim of the work was to investigate the effect of new heterometallic Ge(IV) – 3d-metals complexes with 1-hydroxyethane-1,1-diphosphonic acid and 1,10-phenanthroline on the activity of purified α-L-rhamnosidases produced by Eupenicillium erubescens, Penicillium tardum, Penicillium restrictum, Cryptococcus albidus, α-galactosidase of P. restrictum and proteases with elastolytic and fibrinogenolytic activity of Bacillus sp. The studied compounds (0,1% concentration) activate α-L-rhamnosidase differently depending on its producer. Thus, the activity of α-L-rhamnosidase of E. erubescens was stimulated with [Co(phen)3]4[Ge6(μ-OH)4(μ-O)2(μ-hedp)6]·2СН3СООН·30H2O by 200%, of Penicillium tardum – with [Zn(phen)2(H2O)2]2[Zn(phen)(H2O)4]2[Ge6(μ-OH)4(μ-O)2(μ-hedp)6]·18H2O by 200%, of Penicillium restrictum – with [Ni(phen)3]4[Ge6(μ-OH)4(μ-O)2(μ-hedp)6]·2СН3СООН·26H2O by 67%, of Cryptococcus albidus – wih [Co(phen)3]4[Ge6(μ-OH)4(μ-O)2(μ-hedp)6]·2СН3СООН·30H2O by 40%. The α-galactosidase of Penicillium restrictum was not affected by the investigated compounds. Bacillus sp. IMV B-7883 elastase was activated with [Co(phen)3]4[Ge6(μ-OH)4(μ-O)2(μ-hedp)6]·2СН3СООН·30H2O by 70%, but was totally inhibited with [Fe(phen)3]4[Ge6(μ-OH)4(μ-O)2(μ-hedp)6]·20H2O. The compounds that showed the greatest 200% stimulating effect on the fibrinogenolytic activity of Bacillus sp. IMV B-7883 were [Fe(phen)3]4[Ge6(μ-OH)4(μ-O)2(μ-hedp)6]·20H2O and [Zn(phen)2(H2O)2]2[Zn(phen)(H2O)4]2[Ge6(μ-OH)4(μ-O)2(μ-hedp)6]·18H2O.
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
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.