Перегляд за Автор "Borzova, N. V."

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  • Ескіз
    Документ
    Complexes of biscitratogermanates and biscitratostanates with metals are modifiers of bacillus thuringiensis var. іsraelensis peptidases and penicillium canescens, cladosporium cladosporioides and aspergillus niger α- galactosidases activities
    (2016) Varbanets, L. D.; Nidialkova, N. A.; Borzova, N. V.; Seifullina, Inna Y.; Martsynko, Olena E.; Chebanenko, Olena Anatoliivna; Варбанець, Л. Д.; Нідялкова, Н. А.; Борзова, Н. В.; Сейфулліна, Інна Йосипівна; Марцинко, Олена Едуардівна; Чебаненко, Олена Анатоліївна; Варбанец, Л. Д.; Нидялкова, Н. А.; Борзова, Н. В.; Сейфуллина, Инна Иосифовна; Марцинко, Елена Эдуардовна; Чебаненко, Елена Анатольевна
    The aim of the research was to study the effect of a number of germanium and stanum coordination compounds (compounds 1–8) as modifiers of peptidases and α-galactosidases activity. The coordination compounds of the same type of structure based on chelating ligand that is biologically activities citric acid were investigated as enzymes effectors. Two types of complexes: 1) [M(H2O)6][Ge(НCitr)2]4H2O (M = Mg(1), Mn(2), Co(3), Ni(4), Zn(5)), containing biscitrate-germanate anion ([Ge(НCitr)2]2–), and 2) [M(H2O)6][Sn(НCitr)2]4H2O (M = Mg(6), Co(7), Ni(8)), containing biscitrate-stanate anion and various hexaaquacations ([M(H2O)6]2+, М= Mg, Mn, Co, Ni, Zn) were studied. It is shown that the compound 6, which is biscitrate-stanate complex containing magnesium ions as metal, can be used for the stimulation of B. thuringiensis var. israelensis IMV B-7465 peptidase 1 and peptidase 2 collagenase activity by 20–25%. Compounds 1 (biscitrate-germanate complex containing magnesium ions as metal) and 7 (biscitrate-stanate complex containing cobalt ions as metal), and also compound 6 in a concentration of 0.001% are able to increase elastolytic activity of peptidase 1 by 55–58%. However, compound 7 has shown the greatest activating effect. It increased the elastolytic activity of peptidase 2 by 100–140% (at both tested concentrations). This goes to prove that the compound 7 can be used henceforth as effector of peptidase 2 elastolytic activity. While investigating the effect of the considered coordination compounds on the Penicillium canescens, Cladosporium cladosporioides and Aspergillus niger -galactosidase activity, it has been found that, when using a number of complexes (1–2 and 4–8), there is a slight increase (by 12–20%) of P. canescens enzyme activity, and the maximal effect (~20%, concentration 0.01%) was provided by complex 6.
  • 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
    Властивості α-амілази Aspergillus SP. 55
    (2009) Варбанець, Л. Д.; Авдіюк, К. В.; Борзова, Н. В.; Харкевич, О. С.; Жданова, Н. М.; Сейфулліна, Інна Йосипівна; Марцинко, Олена Едуардівна; Пєсарогло, Олена Георгіївна; Варбанец, Л. Д.; Авдиюк, К. В.; Борзова, Н. В.; Харкевич, Е. С.; Жданова, Н. Н.; Сейфуллина, Инна Иосифовна; Марцинко, Елена Эдуардовна; Песарогло, Алена Георгиевна; Varbanets, L. D.; Avdijuk, К. V.; Borzova, N. V.; Kharkevich, E. S.; Zhdanova, N. N.; Seifullina, Inna Y.; Martsynko, Olena E.; Pesaroglo, Olena G.
    Вивчено вплив різних факторів на процес біосинтезу позаклітинної (α-амілази у Aspergiiius sp. при глибинному культивуванні. Підібрано оптимальний склад поживного середовища: концентрація вуглецю (картопляний крохмаль 1 г/л) та азоту (NaNO3, 0,5 г/л). Ферментний препарат має широкий рН- оптимум активності (4,5—9,0), термооптимум при pH 6,5 — 60 °С, а при pH 4,5 та при 9,0 —50 °С. Показано інгібіторну дію координаційних сполук германію на амілолітичну активність препарату.