Abstrato

Purification and characterization of red beet (beta vulgaris) peroxidase

Sevilay ynal, Ramazan Kalyn, Nalan Ozdemir, Hasan Ozdemir

Red 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.