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Thermostability of glucose oxidase in silica gel obtained by sol–gel method and in solution studied by fluorimetric method

Paper ID Volume ID Publish Year Pages File Format Full-Text
30949 44520 2011 7 PDF Available
Title
Thermostability of glucose oxidase in silica gel obtained by sol–gel method and in solution studied by fluorimetric method
Abstract

The thermostability of glucose oxidase entrapped in silica gel obtained by sol–gel method was studied by thermostimulated fluorescence of FAD at pH 5 and 7 and compared with that of the native enzyme in the solution and at the presence of ethanol. The unfolding temperatures were found to be lower for the enzyme immobilised in gel as compared with the native enzyme but higher as for the enzyme at the presence of ethanol. In gel, the thermal denaturation of glucose oxidase is independent on pH while in solution the enzyme is more stable at pH 5. The investigation the enzyme in different environment by steady-state fluorescence of FAD and tryptophan, synchronous fluorescence and time-resolved fluorescence of tryptophan indicates that the state of the molecule (tertiary structure and molecular dynamics) is different in gel and in solution. The ethanol produced during gel precursor hydrolysis is not the main factor influencing the thermostability of the enzyme but more important are interactions of the protein with the gel lattice.

Keywords
Glucose oxidase; Thermostability; Sol–gel; FAD fluorescence; Tryptophan fluorescence
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Thermostability of glucose oxidase in silica gel obtained by sol–gel method and in solution studied by fluorimetric method
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 103, Issue 1, 4 April 2011, Pages 22–28
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
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Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
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Any Questions? feel free to contact us