Irreversible high pressure inactivation of beta-galactosidase from Kluyveromyces lactis: comparison with thermal inactivation

Journal of Biotechnology
D Cavaille-Lefebvre, D Combes

Abstract

High hydrostatic pressure and high temperature are both shown to induce inactivation of Kluyveromyces lactis beta-galactosidase in deionised water and their respective effects are compared. These two physical parameters lead to similar inactivation kinetics which can be suitably represented by series-type models. The plot of half-lives as a function of pressure is close to the same plot towards temperature. Thus, the same inactivation rate constant can be obtained in two different ways: an increase in pressure at room temperature or an increase in temperature at atmospheric pressure (e.g. 125 MPa at 25 degrees C or 45 degrees C at 0.1 MPa for a kappa 1 value about 28 x 10(-2) min -1). When beta-galactosidase was prepared in 0.1 M potassium phosphate buffer pH 7.3, its stability in extreme conditions of pressure as at high temperature was strongly enhanced. This stabilizing effect of the buffer was essentially attributed to a pH-effect by comparison with the behaviour of the enzyme in a similar buffer but with a 10-fold lower ionic strength.

References

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Citations

Apr 2, 2003·Journal of Biotechnology·Marilyne Noel, Didier Combes
Apr 16, 2003·Critical Reviews in Biotechnology·Andrés Illanes, Lorena Wilson
Nov 18, 2005·Biotechnology Advances·Marta Rubio-Texeira

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