Heat-stability of a proteinase from psychrotrophic Pseudomonas fluorescens P38, chymotrypsin and thermolysin

Richard Owusu, C Doble

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The heat-stabilities of proteinases from a psychrotrophic Psuedomonas fluorescens strain P38 (P38 proteinase), chymotypsin, succinyl-chymotrypsin and thermolysin are compared on the basis of their respective thermoinactivation-rate constants and Arrhenius plots (40–145°C). The Arrhenius plots for P38 proteinase and succinyl-chymotrypsin showed an inversion at 80–90°C characteristic of enzymes showing low-temperature inactivation (LTI). Thermolysin showed a biphasic log k versus 1/T plot consistent with the two-state model for protein and enzyme denaturation. The results are discussed in terms of the kinetics of proteinase autolysis and possible physico-chemical features necessary for LTI.
LanguageEnglish
Pages137
JournalFood Chemistry
Volume51
Issue number2
DOIs
Publication statusPublished - 1994

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Thermolysin
Pseudomonas fluorescens
heat stability
Chymotrypsin
chymotrypsin
Arrhenius plots
Peptide Hydrolases
proteinases
Hot Temperature
inactivation temperature
Protein Denaturation
Autolysis
Denaturation
Temperature
Enzymes
autolysis
Rate constants
Kinetics
kinetics
Proteins

Cite this

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abstract = "The heat-stabilities of proteinases from a psychrotrophic Psuedomonas fluorescens strain P38 (P38 proteinase), chymotypsin, succinyl-chymotrypsin and thermolysin are compared on the basis of their respective thermoinactivation-rate constants and Arrhenius plots (40–145°C). The Arrhenius plots for P38 proteinase and succinyl-chymotrypsin showed an inversion at 80–90°C characteristic of enzymes showing low-temperature inactivation (LTI). Thermolysin showed a biphasic log k versus 1/T plot consistent with the two-state model for protein and enzyme denaturation. The results are discussed in terms of the kinetics of proteinase autolysis and possible physico-chemical features necessary for LTI.",
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Heat-stability of a proteinase from psychrotrophic Pseudomonas fluorescens P38, chymotrypsin and thermolysin. / Owusu, Richard; Doble, C.

Vol. 51, No. 2, 1994, p. 137.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Heat-stability of a proteinase from psychrotrophic Pseudomonas fluorescens P38, chymotrypsin and thermolysin

AU - Owusu, Richard

AU - Doble, C

PY - 1994

Y1 - 1994

N2 - The heat-stabilities of proteinases from a psychrotrophic Psuedomonas fluorescens strain P38 (P38 proteinase), chymotypsin, succinyl-chymotrypsin and thermolysin are compared on the basis of their respective thermoinactivation-rate constants and Arrhenius plots (40–145°C). The Arrhenius plots for P38 proteinase and succinyl-chymotrypsin showed an inversion at 80–90°C characteristic of enzymes showing low-temperature inactivation (LTI). Thermolysin showed a biphasic log k versus 1/T plot consistent with the two-state model for protein and enzyme denaturation. The results are discussed in terms of the kinetics of proteinase autolysis and possible physico-chemical features necessary for LTI.

AB - The heat-stabilities of proteinases from a psychrotrophic Psuedomonas fluorescens strain P38 (P38 proteinase), chymotypsin, succinyl-chymotrypsin and thermolysin are compared on the basis of their respective thermoinactivation-rate constants and Arrhenius plots (40–145°C). The Arrhenius plots for P38 proteinase and succinyl-chymotrypsin showed an inversion at 80–90°C characteristic of enzymes showing low-temperature inactivation (LTI). Thermolysin showed a biphasic log k versus 1/T plot consistent with the two-state model for protein and enzyme denaturation. The results are discussed in terms of the kinetics of proteinase autolysis and possible physico-chemical features necessary for LTI.

U2 - 10.1016/0308-8146(94)90247-X

DO - 10.1016/0308-8146(94)90247-X

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