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Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН (1)

Иностранные журналы библиотеки Института биофизики СО РАН (1)

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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bezrukikh A..., Esimbekova E..., Nemtseva E..., Kratasyuk V..., Shimomura O...
Заглавие : Gelatin and starch as stabilizers of the coupled enzyme system of luminous bacteria NADH:FMN-oxidoreductase-luciferase
Колич.характеристики :5 с
Коллективы : Government of Russian Federation [11.G34.31.0058]; Russian Academy of Sciences [6.8]; Ministry of Education and Science [1762]; Siberian Federal University [1762]
Место публикации : Anal. Bioanal. Chem.: SPRINGER HEIDELBERG, 2014. - Vol. 406, Is. 23. - С. 5743-5747. - ISSN 1618-2642, DOI 10.1007/s00216-014-7987-1. - ISSN 1618-2650
Примечания : Cited References: 14. - The work was supported by the Program of the Government of Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant no. 11.G34.31.0058), the Russian Academy of Sciences (program "Molecular and Cell Biology", grant no. 6.8), and the state contract between the Ministry of Education and Science and Siberian Federal University, no. 1762.
Предметные рубрики: IMMOBILIZATION
CHEMISTRY
Ключевые слова (''Своб.индексиров.''): bacterial luciferase--nadh:fmn-oxidoreductase--bioluminescence--stabilization of enzymes--gelatin--starch
Аннотация: We have studied the effects of a gel-like environment on the characteristics of enzyme preparations based on the coupled enzyme system of luminous bacteria, NADH:FMN-oxidoreductase-luciferase, to design a stable immobilizing reagent for bioluminescent analysis. Natural polymers, gelatin and starch, were used to create a viscous, structured microenvironment. The stability of the coupled enzyme system to such physical and chemical environmental factors as temperature, pH, and ionic strength in gelatin and starch-containing media was examined. It was shown that both gelatin and starch have a stabilizing effect on the enzymes of luminous bacteria under specific conditions. In particular, the enzymes' activity is increased twofold in the presence of 1 and 5 % of gelatin at 20 A degrees C and 25 A degrees C, respectively (temperatures lower than the gel point). Also, the acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol L-1) is observed. At the same time, microenvironments based on either gelatin or starch do not change the enzymes' thermal inactivation rate constants in the temperature range from 25 to 43 A degrees C. Finally, gelatin and starch are suitable for development of a reagent for immobilization of enzymes which would be stable and resistant to physical and chemical environmental conditions.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ganusova M. K., Ivanova-Shor E. A., Shor A. M., Nasluzov V. A., Rubaylo A. I.
Заглавие : Study of Hydration and Hydrolysis of Pu(IV) by the Density Functional Method
Колич.характеристики :8 с
Место публикации : Chem. Sustain. Dev.: PUBLISHING HOUSE RUSSIAN ACAD SCIENCES, SIBERIAN BRANCH, 2017. - Vol. 25, Is. 3. - С. 239-246. - ISSN 0869-8538
Примечания : Cited References:36
Предметные рубрики: FREE-ENERGIES
APPROXIMATION
PLUTONIUM(IV)
CHEMISTRY
ACTINIDES
Ключевые слова (''Своб.индексиров.''): density functional method--plutonium (iv) complexes--the polarizable--continuum model--hydrolysis constants--hydration free energy model--hydrolysis constants--hydration free energy
Аннотация: The structure and the first step of hydrolysis of hydrated Pu(IV) ion in aqueous medium were studied using relativistic density functional theory and the polarizable continuum model (PCM). According to calculations, the Pu(IV) ion was mainly coordinated with eight water molecules. The calculated distance Pu-O of 238-241 pm was in good agreement with the experimental value ((239 +/- 2) pm). It was demonstrated that for the correct replication of constants log K-1(0) of the first hydrolysis step, it was important to use scaling multipliers adequate to the charge of the hydrated complex when constructing the density that included the solvated complex in PCM model. The calculated values of log K-1(0) of -1.1...-0.2 were close to the experimentally defined range (-0.6-0.6). The correct replication of hydrolysis constants allowed considering the calculated range of the hydratation free energies of the Pu(IV) ion of 6070-6157 kJ/mol as a reasonable prediction of experimental values.
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