One‐Step Isolation and Biochemical Characterization of A Novel Peroxidase Enzyme from Jerusalem Artichoke (Helianthus Tuberosus L.)

Abstract

In the present study, a novel peroxidase was purified and characterized from the jerusalem artichoke (Helianthus Tuberosus L.) using an efficient one-step purification method. The purification factor for the jerusalem artichoke peroxidase (POD) was 87.17-fold (with a yield of 13.28 %). Molecular mass and POD purity were controlled with the SDS-PAGE and seen a single band at approximately 47.8 kDa. The optimum parameters (pH, ionic strength, and temperature) for POD activity were investigated and determined as pH 6.5, 0.7 M in phosphate buffer, and 40 °C, respectively. The K M and V max values of the jerusalem artichoke POD were calculated to be 94.33 mM and 12.74 EU/mL.min for guaiacol, and 0.208 mM and 1.481 EU/ mL.min for hydrogen peroxide, respectively. Furthermore, the 4-aminobenzohydrazide was shown to act as a competitive inhibitor of the jerusalem artichoke POD. Finally, molecular docking studies of the 4-aminobenzohydrazide were performed, and the estimated binding energy value was calculated to be À 3.79 kcal/mol.