Akademik Veri Yönetim Sistemi
ASIAN JOURNAL OF CHEMISTRY, cilt.20, sa.3, ss.1927-1936, 2008 (SCI-Expanded, Scopus)
Catalaze (H2O2 center dot H2O2 oxidoreductase: E.C 1.11.1.6) was purified from Coriander (Coriandrum sativum) leaves. The kinetic behaviour and some properties of the enzyme were also investivated. The purification was done at 4 degrees C in two steps: (a) ammonium sulfate fractionation and (b) DEAE-Sephadex A50 ion exchange chomatography. The enzyme was obtained with a yield of 10.67% and had a specific activity of 89.68 EU/mg protein. Optimum pH. stable pH, optimum temperature.. molecular weight, K-M and V-max values for H2O2 was also determined. The overall purification was about 64.06-fold. SDS-PAGE of the purified enzyme showed a single band. Enzymatic activity was spectrophotometrically measured at 240 nm. The molecular mass was estimated to be 60.95 kDa by SDS-PAGE and 58.12 kDa by Sephadex G-150 gel filtration column chromatography. The enzyme had optimum pH at 7.3 and was stable at pH 7.3 in 0.1 M tris-HCl buffer. The optimum temperature was at 30 degrees C. The Km value for H2O2 was 7.87 mM. The V-max value for this substrate was 42.19 EU/mL.