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Mechanisms of heat inactivation of a proteinase from Pseudomonas fluorescens biotype I*

Published online by Cambridge University Press:  01 June 2009

Peter Diermayr ,
Stefan Kroll  and
Henning Klostermeyer
Peter Diermayr
Affiliation:
Süddeutsche Versuchs- und Forschungsanstalt für Milchwirtschaft, D-8050 Freising-Weihenstephan, FRG
Stefan Kroll
Affiliation:
Süddeutsche Versuchs- und Forschungsanstalt für Milchwirtschaft, D-8050 Freising-Weihenstephan, FRG
Henning Klostermeyer
Affiliation:
Süddeutsche Versuchs- und Forschungsanstalt für Milchwirtschaft, D-8050 Freising-Weihenstephan, FRG
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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 Ea 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.

Information

Type
Original Articles
Information
Journal of Dairy Research , Volume 54 , Issue 1 , February 1987 , pp. 51 - 60
Copyright
Copyright © Proprietors of Journal of Dairy Research 1987

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References

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