Pressure-induced activity loss in solid state catalase.
The pressure-induced reductions in the activities of a number of enzymes in the solution state, and more recently in the solid state, have been reported. To further investigate the effect of pressure on proteins in the solid state, the enzyme catalase was used as a model. Compacts containing 150.0 +/- 0.2 mg of catalase powder were prepared on instrumented laboratory presses using various compaction pressures between 0 and 669 MPa. After compaction, a spectrophotometric assay was utilized to determine the pseudo-first-order rate constants for the catalase-catalyzed decomposition of hydrogen peroxide. These rate constants were used to calculate the change in catalase activity. Results indicated a loss in catalase activity of up to 30% at compaction pressures of 251 MPa or greater. While the mechanism which produces the loss of enzyme activity is not clear, a strong linear correlation between enzyme activity and compaction pressure was seen over the range of pressures (0-251 MPa) where the decrease in activity occurred. In addition, compact densities were calculated and correlated to enzyme activity values. This correlation did not appear to be as strong.
Wurster
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Division of Pharmaceutics, College of Pharmacy, University of Iowa, Iowa City 52242, USA.
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D000818:Animals; D002374:Catalase / Q000737:chemistry* / Q000378:metabolism; D002417:Cattle; D006861:Hydrogen Peroxide / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D011312:Pressure; D013056:Spectrophotometry, Ultraviolet
D006861:Hydrogen Peroxide; D002374:Catalase