Literature DB >> 7738799

Pressure-induced activity loss in solid state catalase.

D E Wurster1, R L Ternik.   

Abstract

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.

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Year:  1995        PMID: 7738799     DOI: 10.1002/jps.2600840213

Source DB:  PubMed          Journal:  J Pharm Sci        ISSN: 0022-3549            Impact factor:   3.534


  2 in total

1.  Aggregation of rhDNase occurred during the compression of KBr pellets used for FTIR spectroscopy.

Authors:  H K Chan; B Ongpipattanakul; J Au-Yeung
Journal:  Pharm Res       Date:  1996-02       Impact factor: 4.200

2.  Influence of Tableting on Enzymatic Activity of Papain along with Determination of Its Percolation Threshold with Microcrystalline Cellulose.

Authors:  Manu Sharma; Vinay Sharma; Dipak K Majumdar
Journal:  Int Sch Res Notices       Date:  2014-10-14
  2 in total

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