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

Yemenicioglu, A; ÖZKAN, MEHMET; Velioglu, YAKUP; Cemeroglu, B

doi:10.1007/s002170050260

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

Yemenicioglu A., ÖZKAN M., Velioglu S., Cemeroglu B.

ZEITSCHRIFT FUR LEBENSMITTEL-UNTERSUCHUNG UND-FORSCHUNG A-FOOD RESEARCH AND TECHNOLOGY, cilt.206, sa.4, ss.294-296, 1998 (SCI-Expanded)

Yayın Türü: Makale / Tam Makale
Cilt numarası: 206 Sayı: 4
Basım Tarihi: 1998
Doi Numarası: 10.1007/s002170050260
Dergi Adı: ZEITSCHRIFT FUR LEBENSMITTEL-UNTERSUCHUNG UND-FORSCHUNG A-FOOD RESEARCH AND TECHNOLOGY
Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED)
Sayfa Sayıları: ss.294-296
Anahtar Kelimeler: pinto beans, peroxidase, lipoxygenase, soluble enzymes, heat stability, HEAT-RESISTANT, CAULIFLOWER, ISOENZYME, ENZYME, CORN, PEAS
Ankara Üniversitesi Adresli: Evet

Özet

Thermal inactivation kinetics of crude peroxidase (POX) and lipoxygenase (LOX) in fresh pinto beans were studied over the temperature range of 55-90 degrees 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 degrees 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 degrees C and 49.1 kcal.mol(-1) at 55-90 degrees C.