PURIFICATION AND CHARACTERIZATION OF PEROXIDASE FROM SWEET GOURD (CUCURBITA MOSCHATA LAM. POIRET)

KÖKSAL E., Bursal E., AGGUL A. G., GÜLÇİN İ.

INTERNATIONAL JOURNAL OF FOOD PROPERTIES, cilt.15, sa.5, ss.1110-1119, 2012 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 15 Sayı: 5
  • Basım Tarihi: 2012
  • Doi Numarası: 10.1080/10942912.2010.513216
  • Dergi Adı: INTERNATIONAL JOURNAL OF FOOD PROPERTIES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1110-1119
  • Anahtar Kelimeler: Sweet gourd, Peroxidase, Purification, Chromatography, Electrophoresis, TROUT ONCORHYNCHUS-MYKISS, ERYTHROCYTES IN-VITRO, CARBONIC-ANHYDRASE, OXIDASE, STRESS, ANTIOXIDANT, MELATONIN, ISOZYME
  • Atatürk Üniversitesi Adresli: Evet

Özet

Peroxidase (EC 1.11.1.7; donor: hydrogen peroxide oxidoreductase) is an oxidoreductase enzyme found in many fruits and vegetables. This enzyme was purified from sweet gourd (Cucurbita moschata Lam. Poiret) by ammonium sulphate precipitation and CM-Sephadex ion-exchange chromatography. Furthermore, optimum pH, optimum temperature, optimum ionic strength, stable pH, and stable temperature conditions were determined as 7.2, 50 degrees C, 0.4 M, 8.0, and 40 degrees C, respectively. The molecular weight (M-W) of the enzyme was estimated to be 85 kDa by SDS-PAGE method. The values of K-m and V-max were calculated from the Lineweaver-Burk graph for guaiacol/H2O2 substrate patterns.