Heat inactivation of lipase from psychrotrophic Pseudomonas fluorescens P38: Activation parameters and enzyme stability at low or ultra-high temperatures

Richard K Owusu, A Makhzoum, JS Knapp

Research output: Contribution to journalArticle

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Abstract

A quantitative model is presented for the heat inactivation of enzymes at low or ultra-high temperatures. As a test of its validity, the heat inactivation of crude or partially purified lipase from Pseudomonas fluorescens, strain P38 (P38 lipase) was investigated. The activation energy (ΔE#), enthalpy (ΔH#), entropy (ΔS#) and Gibbs free energy change (ΔG#) for lipase inactivation at 40–140°C were determined. ΔH# for P38 lipase heat inactivation at 40–60°C, 50–80°C and 90–140°C was 170–221 kJ mol−1, −3 − −20 kJ mol–1 and 44–78 kJ mol−1 respectively. Over these temperature intervals ΔS# was 202–380 J mol−1 K−1, −318 − −375 J mol−1 K−1 and −92 − −186 J mol−1 K−1. ΔG# was 100–115 kJ mol−1 for enzyme inactivation at 40–140°C. The results are consistent with different rate-limiting reactions for P38 lipase heat inactivation at low or ultra-high temperatures. Within a narrow range of (intermediate) temperature, a third rate-limiting reaction may lead to ‘low-temperature inactivation’ phenomena. There was qualitative agreement between experimental results and the current model for enzyme heat inactivation.
LanguageEnglish
Pages261
JournalFood Chemistry
Volume44
Issue number4
DOIs
Publication statusPublished - 1992

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enzyme stability
Enzyme Stability
Pseudomonas fluorescens
heat inactivation
Lipase
Hot Temperature
Chemical activation
Temperature
Enzymes
enzyme inactivation
temperature
Low temperature phenomena
inactivation temperature
Gibbs free energy
Entropy
enthalpy
entropy
activation energy
Enthalpy
inactivation

Cite this

@article{4538d861b5ef47a2935e592a5172840b,
title = "Heat inactivation of lipase from psychrotrophic Pseudomonas fluorescens P38: Activation parameters and enzyme stability at low or ultra-high temperatures",
abstract = "A quantitative model is presented for the heat inactivation of enzymes at low or ultra-high temperatures. As a test of its validity, the heat inactivation of crude or partially purified lipase from Pseudomonas fluorescens, strain P38 (P38 lipase) was investigated. The activation energy (ΔE#), enthalpy (ΔH#), entropy (ΔS#) and Gibbs free energy change (ΔG#) for lipase inactivation at 40–140°C were determined. ΔH# for P38 lipase heat inactivation at 40–60°C, 50–80°C and 90–140°C was 170–221 kJ mol−1, −3 − −20 kJ mol–1 and 44–78 kJ mol−1 respectively. Over these temperature intervals ΔS# was 202–380 J mol−1 K−1, −318 − −375 J mol−1 K−1 and −92 − −186 J mol−1 K−1. ΔG# was 100–115 kJ mol−1 for enzyme inactivation at 40–140°C. The results are consistent with different rate-limiting reactions for P38 lipase heat inactivation at low or ultra-high temperatures. Within a narrow range of (intermediate) temperature, a third rate-limiting reaction may lead to ‘low-temperature inactivation’ phenomena. There was qualitative agreement between experimental results and the current model for enzyme heat inactivation.",
author = "Owusu, {Richard K} and A Makhzoum and JS Knapp",
year = "1992",
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pages = "261",
journal = "Food Chemistry",
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Heat inactivation of lipase from psychrotrophic Pseudomonas fluorescens P38: Activation parameters and enzyme stability at low or ultra-high temperatures. / Owusu, Richard K; Makhzoum, A; Knapp, JS.

In: Food Chemistry, Vol. 44, No. 4, 1992, p. 261.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Heat inactivation of lipase from psychrotrophic Pseudomonas fluorescens P38: Activation parameters and enzyme stability at low or ultra-high temperatures

AU - Owusu, Richard K

AU - Makhzoum, A

AU - Knapp, JS

PY - 1992

Y1 - 1992

N2 - A quantitative model is presented for the heat inactivation of enzymes at low or ultra-high temperatures. As a test of its validity, the heat inactivation of crude or partially purified lipase from Pseudomonas fluorescens, strain P38 (P38 lipase) was investigated. The activation energy (ΔE#), enthalpy (ΔH#), entropy (ΔS#) and Gibbs free energy change (ΔG#) for lipase inactivation at 40–140°C were determined. ΔH# for P38 lipase heat inactivation at 40–60°C, 50–80°C and 90–140°C was 170–221 kJ mol−1, −3 − −20 kJ mol–1 and 44–78 kJ mol−1 respectively. Over these temperature intervals ΔS# was 202–380 J mol−1 K−1, −318 − −375 J mol−1 K−1 and −92 − −186 J mol−1 K−1. ΔG# was 100–115 kJ mol−1 for enzyme inactivation at 40–140°C. The results are consistent with different rate-limiting reactions for P38 lipase heat inactivation at low or ultra-high temperatures. Within a narrow range of (intermediate) temperature, a third rate-limiting reaction may lead to ‘low-temperature inactivation’ phenomena. There was qualitative agreement between experimental results and the current model for enzyme heat inactivation.

AB - A quantitative model is presented for the heat inactivation of enzymes at low or ultra-high temperatures. As a test of its validity, the heat inactivation of crude or partially purified lipase from Pseudomonas fluorescens, strain P38 (P38 lipase) was investigated. The activation energy (ΔE#), enthalpy (ΔH#), entropy (ΔS#) and Gibbs free energy change (ΔG#) for lipase inactivation at 40–140°C were determined. ΔH# for P38 lipase heat inactivation at 40–60°C, 50–80°C and 90–140°C was 170–221 kJ mol−1, −3 − −20 kJ mol–1 and 44–78 kJ mol−1 respectively. Over these temperature intervals ΔS# was 202–380 J mol−1 K−1, −318 − −375 J mol−1 K−1 and −92 − −186 J mol−1 K−1. ΔG# was 100–115 kJ mol−1 for enzyme inactivation at 40–140°C. The results are consistent with different rate-limiting reactions for P38 lipase heat inactivation at low or ultra-high temperatures. Within a narrow range of (intermediate) temperature, a third rate-limiting reaction may lead to ‘low-temperature inactivation’ phenomena. There was qualitative agreement between experimental results and the current model for enzyme heat inactivation.

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