Inactivation characteristics shown by enzymes and bacteria treated with far-infrared radiative heating
| Autor: | Koji Sagara, Masaru Shimizu, Jun Sawai, Atsushi Hashimoto, Hideo Igarashi |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
chemistry.chemical_classification
biology Chemistry Triacylglycerol lipase Activation energy Thermal conduction medicine.disease_cause Industrial and Manufacturing Engineering Enzyme assay Reaction rate constant Enzyme biology.protein medicine Biophysics Organic chemistry Lipase Escherichia coli Food Science |
| Zdroj: | International Journal of Food Science and Technology. 38:661-667 |
| ISSN: | 1365-2621 0950-5423 |
| DOI: | 10.1046/j.1365-2621.2003.00717.x |
| Popis: | Summary The inactivation of the enzymes lipase and α-amylase were studied during treatment by far-infrared (FIR) radiative heating and compared with activity changes due to heating by thermal conduction. The decrease in enzyme activity was found to be largely similar for the two processes, as long as the temperature profiles of the enzyme solutions were identical during heating. The inactivation of α-amylase was compared with bacterial death (Escherichia coli) using both FIR and conductive heating. The inactivation energy required to inactivate enzymes was an order of magnitude lower than that for inactivation of E. coli and the death rate constants of bacteria (kdeath) became larger than the inactivation rate constant of the enzyme (ken) at about 50 °C or higher. At the given temperatures, the kdeath values for FIR was larger than kdeath values for conductive heating, suggesting that FIR heating may allow a given pasteurization target level to be achieved at lower temperatures than by conductive heating, while maintaining enzyme activity levels. |
| Databáze: | OpenAIRE |
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