ISSN:
1745-4514
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
The enzymes, chymotrypsin, trypsin, collagenase and cathepsin C, as well as the protease inhibitor, α2-macroglobulin, have been shown to be susceptible to hydrostatic pressure inactivation. a2-Macroglobulin lost about 15% activity at a pressure of 2,000 atm and as much as 80% at 3,000 atm pressure applied for 1 h in both cases. Thermal stability studies also indicated the protein to be completely denatured at about 75C. The enzymes were also inactivated to various extents depending on the amount of pressure and the duration of application, The degree of susceptibility to pressures ranging between 2,000–4,000 atm applied for time periods ranging from 5–60 min was found to be as follows: chymotrypsin 〈 cathepsin 〈 trypsin 〈 collagenase. The hydrostatic pressure effects were irreversible when pressure-treated enzymes were stored at room temperature (20–25C), but showed various levels of reactivation when stored at refrigerated temperatures (4–7C).
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1745-4514.1994.tb00511.x
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