Abstract
Purification and characterization of red beet (beta vulgaris) peroxidase
Author(s): Sevilay ynal, Ramazan Kalyn, Nalan Ozdemir, Hasan OzdemirRed beet (Beta vulgaris) is an important source of dietary having various bioactive compounds. In this study, a peroxidase was purified for the first time from native red beet (Beta vulgaris) in a single step using 4- aminobenzohydrazide affinity chromatography and characterized biochemically. The molecular weight of the purified enzyme was calculated approximately as 160 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and a single bandwas observed.As a result of the kinetic studies on the enzyme; optimum pH, optimum ionic strength, optimum temperature and stable pH were determined as 6.5, 0.7 M, 70 °C, 6.5, respectively for red beet (Beta vulgaris L.). Red beet (Beta vulgaris) peroxidase showed KM and Vmax values of 9.09mMand 1.38 EU/mL.min for guaiacol/H2O2, respectively. Also, inhibitory effect of 4- aminobenzohydrazide on purified peroxidase enzymewas examined in vitro condition. The IC50 and Ki values were calculated as 0.047 and 0.78±0.17 mM, respectively.
