Thermal stabilities of peroxidases from fresh pinto beans

Yemenicioglu A., ÖZKAN M., Cemeroglu B.

JOURNAL OF FOOD SCIENCE, cilt.63, sa.6, ss.987-990, 1998 (SCI-Expanded, Scopus) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 63 Sayı: 6
  • Basım Tarihi: 1998
  • Doi Numarası: 10.1111/j.1365-2621.1998.tb15839.x
  • Dergi Adı: JOURNAL OF FOOD SCIENCE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.987-990
  • Anahtar Kelimeler: peroxidase, pinto beans, heat activation, heat inactivation, purification, POLYPHENOL OXIDASE, APPLE POLYPHENOLOXIDASE, HORSERADISH-PEROXIDASE, INACTIVATION KINETICS, HEAT INACTIVATION, ISOENZYMES, VEGETABLES, PURIFICATION, ASPARAGUS, RESISTANT
  • Ankara Üniversitesi Adresli: Evet

Özet

Heat stabilities of crude and partially purified soluble (SPOX), ionically bound (IPOX) and total peroxidase (TPOX) from fresh pinto beans were investigated at 55-90 degrees C, Heat inactivation of peroxidase (POX) followed first-order reaction kinetics. Each inactivation curve consisted of two linear parts: initial rapid inactivation (heat-labile) followed by slower inactivation (heat-stable). IPOX showed activation during heat treatment with a highly heat-stable isoenzyme (D-90=40 min) which was more heat-stable than SPOX. Activation energies for heat-stable parts of crude IPOX and SPOX were, respectively, 12.1 and 36.4 kcal.mol-1 with z values 45.4 and 14.1C degrees. Heat stable SPOX isoenzymes (D-70=22.6) were obtained by 65-95% (NH4)(2)SO4 precipitation from crude SPOX. Two POX fractions (F1 and F2) were separated from TPOX by ion-exchange chromatography.