Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength

Jorge A. Saraiva, Jorge C. Oliveira, M. Adilia Lemos, Marc E. Hendrickx

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The thermal inactivation of horseradish peroxidase was studied in sodium phosphate buffer solutions and in pure water at pH 7 in the temperature range of 70–95°C. The sodium phosphate ions concentration affected both the thermostability and the kinetic patterns and had a stabilizing effect. The gradual change observed at low concentrations made a series-type mechanism theoretically more coherent with the experimental observations than the conventionally applied two-fraction model. In water the kinetics is apparently First order at high temperatures, while the results obtained at 25°C support the occurrence of a series-type inactivation mechanism. The pH and enzyme concentration also affect the inactivation proFile, supporting the conclusion that the thermal inactivation is not a monomolecular process with respect to protein concentration.
Original languageEnglish
Pages (from-to)223–231
Number of pages9
JournalInternational Journal of Food Science and Technology
Volume31
Issue number3
DOIs
Publication statusPublished - May 1996

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sodium phosphate
heat inactivation
Horseradish Peroxidase
ionic strength
Ionic strength
Osmolar Concentration
inactivation
Buffers
peroxidase
Phosphates
buffers
Hot Temperature
Sodium
kinetics
Kinetics
Temperature
Water
thermal stability
temperature
Enzymes

Cite this

@article{b46d553bb1bd4d1685ec3ead55f72139,
title = "Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength",
abstract = "The thermal inactivation of horseradish peroxidase was studied in sodium phosphate buffer solutions and in pure water at pH 7 in the temperature range of 70–95°C. The sodium phosphate ions concentration affected both the thermostability and the kinetic patterns and had a stabilizing effect. The gradual change observed at low concentrations made a series-type mechanism theoretically more coherent with the experimental observations than the conventionally applied two-fraction model. In water the kinetics is apparently First order at high temperatures, while the results obtained at 25°C support the occurrence of a series-type inactivation mechanism. The pH and enzyme concentration also affect the inactivation proFile, supporting the conclusion that the thermal inactivation is not a monomolecular process with respect to protein concentration.",
author = "Saraiva, {Jorge A.} and Oliveira, {Jorge C.} and Lemos, {M. Adilia} and Hendrickx, {Marc E.}",
year = "1996",
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language = "English",
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Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength. / Saraiva, Jorge A.; Oliveira, Jorge C.; Lemos, M. Adilia; Hendrickx, Marc E.

In: International Journal of Food Science and Technology, Vol. 31, No. 3, 05.1996, p. 223–231.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength

AU - Saraiva, Jorge A.

AU - Oliveira, Jorge C.

AU - Lemos, M. Adilia

AU - Hendrickx, Marc E.

PY - 1996/5

Y1 - 1996/5

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AB - The thermal inactivation of horseradish peroxidase was studied in sodium phosphate buffer solutions and in pure water at pH 7 in the temperature range of 70–95°C. The sodium phosphate ions concentration affected both the thermostability and the kinetic patterns and had a stabilizing effect. The gradual change observed at low concentrations made a series-type mechanism theoretically more coherent with the experimental observations than the conventionally applied two-fraction model. In water the kinetics is apparently First order at high temperatures, while the results obtained at 25°C support the occurrence of a series-type inactivation mechanism. The pH and enzyme concentration also affect the inactivation proFile, supporting the conclusion that the thermal inactivation is not a monomolecular process with respect to protein concentration.

U2 - 10.1046/j.1365-2621.1996.00342.x

DO - 10.1046/j.1365-2621.1996.00342.x

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