Thermochimica Acta, ( ISI ), Volume (235), No (2), Year (1994-4) , Pages (189-196)

Title : ( Thermodynamic denaturation of glucose oxidase in aqueous dodecyl trimethyl ammonium bromide solution between 25 and 65°C )

Authors: Mohammad Reza Housaindokht , A. A. Mosavi-Movahedi ,

Citation: BibTeX | EndNote

Abstract

The denaturation of glucose oxidase has been studied as a function of dodecyl trimethyl ammonium bromide (DTAB) concentration at temperatures between 25 and 65°C, with 2.5 mM phosphate buffer and pH 6.4. DTAB was found to be very effective in denaturing glucose oxidase, normally resistent to other denaturing agents. At 55°C, the enzyme is expected to have minimum stability in the hydrocarbon environment provided by the detergent. In an otherwise identical situation, when water surrounds the protein, maximum stability is suggested. These predictions are made using the Gibbs free energies of the transition in water ΔGD(H2O), and in a hydrophobic environment ΔGD(hc). The values of ΔGD(H2O) and ΔGD(hc) were 26.84 and -180.2 kJ

Keywords

Thermodynamic denaturation of glucose
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@article{paperid:1015093,
author = {Housaindokht, Mohammad Reza and A. A. Mosavi-Movahedi},
title = {Thermodynamic denaturation of glucose oxidase in aqueous dodecyl trimethyl ammonium bromide solution between 25 and 65°C},
journal = {Thermochimica Acta},
year = {1994},
volume = {235},
number = {2},
month = {April},
issn = {0040-6031},
pages = {189--196},
numpages = {7},
keywords = {Thermodynamic denaturation of glucose},
}

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%0 Journal Article
%T Thermodynamic denaturation of glucose oxidase in aqueous dodecyl trimethyl ammonium bromide solution between 25 and 65°C
%A Housaindokht, Mohammad Reza
%A A. A. Mosavi-Movahedi
%J Thermochimica Acta
%@ 0040-6031
%D 1994

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