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

doi:10.1046/j.1365-2621.1996.00342.x

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 journal › Article › peer-review

28 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 language	English
Pages (from-to)	223–231
Number of pages	9
Journal	International Journal of Food Science and Technology
Volume	31
Issue number	3
DOIs	https://doi.org/10.1046/j.1365-2621.1996.00342.x
Publication status	Published - May 1996

Keywords

Enzyme inactivation
Kinetic models

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10.1046/j.1365-2621.1996.00342.x

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@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",

month = may,

doi = "10.1046/j.1365-2621.1996.00342.x",

language = "English",

volume = "31",

pages = "223–231",

journal = "International Journal of Food Science and Technology",

issn = "0950-5423",

publisher = "Wiley-Blackwell",

number = "3",

}

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

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

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

N2 - 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.

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

M3 - Article

SN - 0950-5423

VL - 31

SP - 223

EP - 231

JO - International Journal of Food Science and Technology

JF - International Journal of Food Science and Technology

IS - 3

ER -

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

Abstract

Keywords

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