THERMAL INACTIVATION KINETICS OF PEROXIDASE AND LIPOXYGENASE FROM FRESH PINTO BEANS (PHASEOLUS-VULGARIS)

Authors
YEMENICIOGLU A OZKAN M VELIOGLU S CEMEROGLU B
Citation
A. Yemenicioglu et al., THERMAL INACTIVATION KINETICS OF PEROXIDASE AND LIPOXYGENASE FROM FRESH PINTO BEANS (PHASEOLUS-VULGARIS), ZEITSCHRIFT FUR LEBENSMITTEL-UNTERSUCHUNG UND-FORSCHUNG A-FOOD RESEARCH AND TECHNOLOGY, 206(4), 1998, pp. 294-296
Citations number
27
Categorie Soggetti
Food Science & Tenology
Journal title
ZEITSCHRIFT FUR LEBENSMITTEL-UNTERSUCHUNG UND-FORSCHUNG A-FOOD RESEARCH AND TECHNOLOGY → ACNP
ISSN journal
14314630
Volume
206
Issue
4
Year of publication
1998
Pages
294 - 296
Database
ISI
SICI code
1431-4630(1998)206:4<294:TIKOPA>2.0.ZU;2-#
Abstract
Thermal inactivation kinetics of crude peroxidase (POX) and lipoxygena se (LOX) in fresh pinto beans were studied over the temperature range of 55-90 degrees C. The inactivation of both enzymes followed first-or der kinetics. The biphasic inactivation curves for POX indicate the ex istence of several isoenzymes of varying heat stability. In the temper ature range of 55-70 degrees C, the activation energies (E-a) of POX w ere 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 a n E-a value of 42.26 kcal.mol(-1) at 55-75 degrees C and 49.1 kcal.mol (-1) at 55-90 degrees C.