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• W2018565792 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." @default.
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• W2018565792 date "1998-04-01" @default.
• W2018565792 modified "2023-09-27" @default.
• W2018565792 title "Irreversible high pressure inactivation of β-galactosidase from Kluyveromyces lactis: Comparison with thermal inactivation" @default.
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• W2018565792 doi "https://doi.org/10.1016/s0168-1656(98)00007-8" @default.
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