Thermal inactivation kinetics of peroxidase and lipoxygenase from fresh pinto beans (Phaseolus vulgaris) |
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Authors: | Ahmet Yemeniciolu Mehmet ?zkan Sedat Veliolu and B Cemerolu |
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Affiliation: | (1) Department of Food Engineering, Faculty of Agriculture, Ankara University, Diskapi-Ankara 06110, Turkey, TR |
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Abstract: | 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 (E
a) 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 E
a value of 42.26 kcal·mol–1 at 55–75°C and 49.1 kcal·mol–1 at 55–90°C.
Received: 28 July 1997 / Revised version: 16 October 1997 |
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Keywords: | Pinto beans Peroxidase Lipoxygenase Soluble enzymes Heat stability |
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