Soluble and immobilized catalase. Effect of pressure and inhibition on kinetics and deactivation.
This article examines the effect of pressure on the steady-state kinetics and long-term deactivation of the enzyme catalase supported on porous alumina. The reaction studied is the decomposition of hydrogen peroxide. The results of studies carried out in a continuous stirred-tank reactor under isothermal conditions are presented and compared with results obtained for soluble catalase. For soluble catalase, it is found that in the range of pressures studied, the oxygen flow rate increases with increase in pressure up to a certain value and then decreases. Hydrogen peroxide concentration appears to have a strong influence on pressure effects. With immobilized catalase, the pressure effects are not as prominent. Fluorescent microscopy studies of the immobilized enzyme suggest that this is probably because of pore diffusional limitations.
Department of Chemical Engineering, University of New Hampshire, Durham 03824.
P T
PT
Vasudevan
D S
DS
Thakur
D000537:Aluminum Oxide; D000818:Animals; D002374:Catalase / Q000037:antagonists & inhibitors* / Q000378:metabolism*; D002417:Cattle; D004789:Enzyme Activation; D004800:Enzymes, Immobilized; D016650:Fluorescein-5-isothiocyanate; D005456:Fluorescent Dyes; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D010100:Oxygen / Q000378:metabolism; D011312:Pressure; D012995:Solubility; D013696:Temperature
D004800:Enzymes, Immobilized; D005456:Fluorescent Dyes; D002374:Catalase; D016650:Fluorescein-5-isothiocyanate; D000537:Aluminum Oxide; D010100:Oxygen