Перегляд за Автор "Gudzenko, O. V."

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  • Ескіз
    Документ
    Different-ligand and different-metal xylaratogermanates as effectors of Penicillium restrictum IM V F-100139 α-L-rhamnosidase and α-galactosidase
    (2021) Gudzenko, O. V.; Borzova, N. V.; Varbanets, L. D.; Seifullina, Inna Y.; Chebanenko, Olena A.; Martsynko, Olena E.; Сейфулліна, Інна Йосипівна; Чебаненко, Олена Анатоліївна; Марцинко, Олена Едуардівна; Сейфуллина, Инна Иосифовна; Чебаненко, Елена Анатольевна; Марцинко, Елена Эдуардовна
    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 differentligand 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.
  • Ескіз
    Документ
    The influence of coordinative tartrate and malatogermanate compounds on the activity of α-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus
    (2020) Gudzenko, O. V.; Varbanets, L. D.; Seifullina, Inna Y.; Chebanenko, Olena A.; Martsynko, Olena E.; Аfanasenko, Е. V.; Сейфулліна, Інна Йосипівна; Чебаненко, Олена Анатоліївна; Марцинко, Олена Едуардівна; Сейфуллина, Инна Иосифовна; Чебаненко, Елена Анатольевна; Марцинко, Елена Эдуардовна
    Recently enzyme preparations of microbial origin become increasingly important in different industries. Preparations of α-L-rhamnosidase are used in the pharmaceutical industry as well as in scientific work as a tool for analytical research. We have obtained purified α-L-rhamnosidase preparations from Penicillium tardum, Eupenicillium erubescens and Cryptococcus albidus microorganism strains which are effective enzyme producers. The aim of the study was to estimate the ability of germanium coordination compounds to enhance enzyme catalytic activity. The effects of 11 heterometal mixed ligand tartrate (malate-)germanate compounds at 0.01 and 0.1% concentration on the activity of α-L-rhamnosidase preparations from Penicillium tardum IMV F-100074, Eupenicillium erubescens and Cryptococcus albidus 1001 were studied at 0.5 and 24 h exposition. The inhibitory effect of [Ni(bipy)3]4[{Ge2(OH )2(Tart)2}3Cl2]·15H2 on P. tardum α-L-rhamnosidase was revealed. All studied compounds except [CuCl(phen)2][Ge(OH )(HMal)2] were shown to increase activity of P. tardum α-L-rhamnosidase at a longer term of exposition. Activity of E. erubescens α-L-rhamnosidase was shown to be stimulated by d-metal cation-free compounds. C. albidus α-L-rhamnosidase occurred to be insensitive to all compounds studied.