Kalin, Ramazan2026-03-262026-03-2620232365-654910.1002/slct.2022047322-s2.0-85147858332https://doi.org/10.1002/slct.202204732https://hdl.handle.net/20.500.14901/3165In 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 degrees 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 -3.79 kcal/mol.eninfo:eu-repo/semantics/closedAccess4-AminobenzohidrazideAffinity ChromatographyJerusalem ArtichokePeroxidasePurificationArticle