Purification and Biochemical Characterization of Peroxidase Isolated from White Cabbage (Brassica Oleracea var. capitata f. alba)
INTERNATIONAL JOURNAL OF FOOD PROPERTIES, cilt.18, sa.10, ss.2099-2109, 2015 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 18 Sayı: 10
- Basım Tarihi: 2015
- Doi Numarası: 10.1080/10942912.2014.963868
- Dergi Adı: INTERNATIONAL JOURNAL OF FOOD PROPERTIES
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.2099-2109
- Anahtar Kelimeler: White cabbage, Affinity chromatography, Enzyme kinetics, Brassica oleracea, Enzyme purification, Peroxidase
- Erciyes Üniversitesi Adresli: Evet
Özet
Peroxidase enzyme was purified for the first time from white cabbage (Brassica oleracea var. capitata f. alba) in a single step using affinity chromatography and some biochemical characteristics of the purified enzyme were determined. The peroxidase was purified 24.7-fold with an overall recovery of 4.3% and a specific activity of 964.5. The molecular weight of the purified peroxidase was approximately 73.2 kDa as calculated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and it showed maximum activity at pH 6.5 and 30 degrees C. For the guaiacol substrate, the K-M and V-max values were found as 3.19 mM and 0.2 EU/mL, respectively. Additionally, the IC50 and K-i values were determined as 0.517 and 0.994 +/- 0.453 mM, respectively, for 4-aminobenzohydrazide. 4-amino benzohydrazide showed non-competitive inhibition.