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• W1998883665 abstract "Summary Heat inactivation of a metalloproteinase, isolated from Pseudomonas fluorescens biotype I strain 112, was investigated in the temperature ranges 50–60 °C and 90–140 °C. At 90 °C the denaturation of the enzyme followed first-order kinetics with a decimal reduction time of 110 min and a velocity constant K of 3·5 × 10 −4 s −1 . Activation energy E a was 100 kJ/mol for this temperature range. In the 50–60 °C region the proteinase was inactivated by autolysis, as shown by electrophoresis and gel filtration. At 55 °C the decimal reduction time was ∼ 22 s, at 57 °C it was 8 s. Rapid inactivation at 55 °C was only possible if the enzyme was heated from lower temperatures, but not if cooled down from 90 °C. This is due to a conformational change of the protein at this temperature. A model for the description of heat inactivation in the two temperature ranges is proposed." @default.
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• W1998883665 date "1987-02-01" @default.
• W1998883665 modified "2023-09-24" @default.
• W1998883665 title "Mechanisms of heat inactivation of a proteinase from <i>Pseudomonas fluorescens</i> biotype I" @default.
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• W1998883665 doi "https://doi.org/10.1017/s002202990002519x" @default.
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