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

Abstract

AbstractIn 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 KM and Vmax 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 −3.79 kcal/mol.