Premium
The effect of oxygen upon the kinetics of glucose oxidase inactivation
Author(s) -
Venugopal Ramakrishnan,
Saviue Bradley A.
Publication year - 1993
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.5450710613
Subject(s) - oxygen , chemistry , partial pressure , glucose oxidase , oxidase test , enzyme , kinetics , limiting oxygen concentration , catalysis , biochemistry , organic chemistry , physics , quantum mechanics
The effect of oxygen upon the inactivation rate of glucose oxidase was studied. Tests on enzyme stability during catalytic turnover were conducted under a range of oxygen partial pressures. A standard activity assay was used to monitor changes in glucose oxidase activity. Studies revealed that oxygen influenced the inactivation of glucose oxidase. Inactivation rates during catalytic turnover ranged between 0.01143 +/‐ 0.0016 h ‐1 under 10 kPa oxygen to 0.04879 +/‐ 0.0023 h ‐1 under 101 kPa oxygen. Statistically different inactivation rates were obtained at oxygen partial pressures of 10,15, 21, 51, and 76 kPa. The enzymatic turnover number decreased from 11.0 X 10 4 to 5.7 X 10 4 when the oxygen partial pressure increased from 10 to 101 kPa, suggesting that enzyme utilization was most efficient at low oxygen partial pressures (<15 kPa).