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

Richard Owusu; C Doble

doi:10.1016/0308-8146(94)90247-X

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

Richard Owusu, C Doble

Faculty Of Life & Health Sciences

Research output: Contribution to journal › Article › peer-review

8 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.

Original language	English
Pages (from-to)	137
Journal	Food Chemistry
Volume	51
Issue number	2
DOIs	https://doi.org/10.1016/0308-8146(94)90247-X
Publication status	Published (in print/issue) - 1994

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

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.",

author = "Richard Owusu and C Doble",

year = "1994",

doi = "10.1016/0308-8146(94)90247-X",

language = "English",

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pages = "137",

journal = "Food Chemistry",

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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

M3 - Article

VL - 51

SP - 137

JO - Food Chemistry

JF - Food Chemistry

IS - 2

ER -

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

Abstract

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