Akademik Veri Yönetim Sistemi
INTERNATIONAL JOURNAL OF FOOD PROPERTIES, cilt.20, ss.1944-1953, 2017 (SCI-Expanded)
In this study, a cationic soluble peroxidase (POD) was homogeneously purified and biochemically characterized. The enzyme purification involved the combination of (NH4)(2)SO4 precipitation, CM-Sephadex cation exchange, and gel filtration chromatography. The purity of the enzyme was examined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, and one single prominent band was obtained with a molecular weight of approximately 45 kDa. The thermal and pH stability showed that the enzyme was stable at pH 5.0 and at 40 degrees C, respectively. The activity remained stable at pH 4.0 at least for 10days. K-m and V-max values were calculated from Lineweaver-Burk graph for each substrate. POD exhibited K-m values of 0.0154 and 0.065mM for guaiacol and H2O2, respectively. The enzyme was highly inhibited by sodium azide. This study could enrich the literature regarding the properties of POD from haricot bean that could be applicable to biomedical analysis.