期刊
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
卷 103, 期 1, 页码 22-28出版社
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2011.01.007
关键词
Glucose oxidase; Thermostability; Sol-gel; FAD fluorescence; Tryptophan fluorescence
资金
- Polish Ministry of Science and Higher Education [N N312 257234]
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. (C) 2011 Elsevier B.V. All rights reserved.
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