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The effect of oxygen upon the kinetics of enzyme inactivation: In vitro investigations using glutamine synthetase
Author(s) -
Saville Bradley A.,
Persi Steven
Publication year - 1992
Publication title -
the canadian journal of chemical engineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.404
H-Index - 67
eISSN - 1939-019X
pISSN - 0008-4034
DOI - 10.1002/cjce.5450700614
Subject(s) - partial pressure , oxygen , enzyme , chemistry , glutamine synthetase , glutamine , kinetics , oxidase test , enzyme kinetics , biochemistry , enzyme assay , in vitro , nuclear chemistry , amino acid , active site , organic chemistry , physics , quantum mechanics
Abstract The relationship between enzyme inactivation and the concentration of oxygen in the reaction environment was studied using glutamine synthetase. Batch incubations of the enzyme were conducted under different oxygen partial pressures in a mixed‐function oxidase model system. Enzyme activity was monitored using a transferase reaction assay. Studies showed that oxygen was necessary for inactivation to occur. Furthermore, for oxygen partial pressures up to 61kPa, the rate of inactivation increased linearly with partial pressure. Rates of inactivation ranged from 0.0172+/−0.0038 min ‐1 at 15 kPa to 0.0591+/−0.0045 min ‐1 at 61 kPa. However, at partial pressures of 61, 81, and 101 kPa, rates of inactivation were statistically identical.