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полный	информационный	краткий

Поисковый запрос: (<.>S=IMMOBILIZATION<.>)

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Gelatin and starch as stabilizers of the coupled enzyme system of luminous bacteria NADH:FMN-oxidoreductase-luciferase [Text] / A. . Bezrukikh [et al.] // Anal. Bioanal. Chem. - 2014. - Vol. 406, Is. 23. - P5743-5747, DOI 10.1007/s00216-014-7987-1. - 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. . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
IMMOBILIZATION
CHEMISTRY
Кл.слова (ненормированные):
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.

WOS
Держатели документа:
[Bezrukikh, Anna
Esimbekova, Elena
Nemtseva, Elena
Kratasyuk, Valentina
Shimomura, Osamu] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
[Esimbekova, Elena
Nemtseva, Elena
Kratasyuk, Valentina] Inst Biophys SB RAS, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bezrukikh, A...; Esimbekova, E...; Nemtseva, E...; Kratasyuk, V...; Shimomura, O...; Government of Russian Federation [11.G34.31.0058]; Russian Academy of Sciences [6.8]; Ministry of Education and Science [1762]; Siberian Federal University [1762]

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