Thermal inactivation kinetics of peroxidase and lipoxygenase from fresh pinto beans (Phaseolus vulgaris)

被引：0
|
作者：
Ahmet Yemenicioğlu
Mehmet Özkan
Sedat Velioğlu
B. Cemeroğlu
机构：
[1] Department of Food Engineering,
[2] Faculty of Agriculture,undefined
[3] Ankara University,undefined
[4] Diskapi-Ankara 06110,undefined
[5] Turkey,undefined
来源：
Zeitschrift für Lebensmitteluntersuchung und -Forschung A | 1998年 / 206卷
关键词：
Key words Pinto beans; Peroxidase; Lipoxygenase; Soluble enzymes; Heat stability;
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学科分类号：
摘要：
 Thermal inactivation kinetics of crude peroxidase (POX) and lipoxygenase (LOX) in fresh pinto beans were studied over the temperature range of 55–90°C. The inactivation of both enzymes followed first-order kinetics. The biphasic inactivation curves for POX indicate the existence of several isoenzymes of varying heat stability. In the temperature range of 55–70°C, the activation energies (Ea) of POX were 46.5 kcal·mol–1 for the heat-labile portion and 37.6 kcal·mol–1 for the heat-stable portion. On the other hand, the LOX enzyme had an Ea value of 42.26 kcal·mol–1 at 55–75°C and 49.1 kcal·mol–1 at 55–90°C.
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页码：294 / 296
页数：2
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