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