IRIS publication 43338894
Influence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution
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TY - JOUR - Lemos, MA,Oliveira, JC,Saraiva, JA - 2000 - Unknown - LWT - Food Science and Technology - Influence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution - Validated - () - enzyme inactivation kinetic modelling protein thermal denaturation ALPHA-AMYLASE BACILLUS-LICHENIFORMIS REACTIVATION STABILITY - 33 - 362 - 368 - The thermal inactivation of horseradish peroxidase in aqueous solution was studied in the pH range of 3.0 to 12.5, at temperatures ranging from 40 degrees C to 95 degrees C. The data were well fitted by a double exponential mode. The enzyme showed highest stability around neutral pH and the stability was particularly decreased above pH 11. The z value of the less labile fraction at pH 11.5 to 12.5 (temperatures from 40 to 65 degrees C) and of the more labile fraction at pH 3-4 (temperatures from 65 to 85 degrees C) were close to 10 degrees C, making these systems suitable as time-temperature integrators for assessing microbial lethality in thermal processing of low-acid foods, particularly if they can be stabilized further without affecting their low z-value. (C) 2000 Academic Press. DA - 2000/NaN ER -
BIBTeX format for JabRef and similar
@article{V43338894, = {Lemos, MA and Oliveira, JC and Saraiva, JA }, = {2000}, = {Unknown}, = {LWT - Food Science and Technology}, = {Influence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution}, = {Validated}, = {()}, = {enzyme inactivation kinetic modelling protein thermal denaturation ALPHA-AMYLASE BACILLUS-LICHENIFORMIS REACTIVATION STABILITY}, = {33}, pages = {362--368}, = {{The thermal inactivation of horseradish peroxidase in aqueous solution was studied in the pH range of 3.0 to 12.5, at temperatures ranging from 40 degrees C to 95 degrees C. The data were well fitted by a double exponential mode. The enzyme showed highest stability around neutral pH and the stability was particularly decreased above pH 11. The z value of the less labile fraction at pH 11.5 to 12.5 (temperatures from 40 to 65 degrees C) and of the more labile fraction at pH 3-4 (temperatures from 65 to 85 degrees C) were close to 10 degrees C, making these systems suitable as time-temperature integrators for assessing microbial lethality in thermal processing of low-acid foods, particularly if they can be stabilized further without affecting their low z-value. (C) 2000 Academic Press.}}, source = {IRIS} }
Data as stored in IRIS
AUTHORS | Lemos, MA,Oliveira, JC,Saraiva, JA | ||
YEAR | 2000 | ||
MONTH | Unknown | ||
JOURNAL_CODE | LWT - Food Science and Technology | ||
TITLE | Influence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution | ||
STATUS | Validated | ||
TIMES_CITED | () | ||
SEARCH_KEYWORD | enzyme inactivation kinetic modelling protein thermal denaturation ALPHA-AMYLASE BACILLUS-LICHENIFORMIS REACTIVATION STABILITY | ||
VOLUME | 33 | ||
ISSUE | |||
START_PAGE | 362 | ||
END_PAGE | 368 | ||
ABSTRACT | The thermal inactivation of horseradish peroxidase in aqueous solution was studied in the pH range of 3.0 to 12.5, at temperatures ranging from 40 degrees C to 95 degrees C. The data were well fitted by a double exponential mode. The enzyme showed highest stability around neutral pH and the stability was particularly decreased above pH 11. The z value of the less labile fraction at pH 11.5 to 12.5 (temperatures from 40 to 65 degrees C) and of the more labile fraction at pH 3-4 (temperatures from 65 to 85 degrees C) were close to 10 degrees C, making these systems suitable as time-temperature integrators for assessing microbial lethality in thermal processing of low-acid foods, particularly if they can be stabilized further without affecting their low z-value. (C) 2000 Academic Press. | ||
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