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Trofimova D., Kamyshny A., Magdassi S., Levashov A.

Influence of chemical modification on thermostability of glucose oxidase and formate dehydrogenase

Abstract

Stability of native and modified glucose oxidase from Aspergillus Niger (GOD) and formate dehydrogenase from the methylotropic bacteria Pseudomonas sp. 101 (FDH) were studied in water systems. It was found, thermal inactivation of the enzymes both native and modified follows near first order. Modification of GOD does not affect on structure and stability. But in case of FDH its stability hydrophobil-lipofilic balance – sensitive. The hydrophylization of FDH (by glycosilation) decreases the stability of this enzyme in 5 times. In contrast hydrophobization of FDH (by acylation) increase the stability of this enzyme in 2 times.
Moscow University Chemistry Bulletin.
2003, Vol. 44, No. 1, P. 48
   

Copyright (C) Chemistry Dept., Moscow State University, 2002
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