Kavaz, Neslihan MacitErel, DenizKorkmaz, Isil NihanGerni, SerpilAbul, NurgulBayrak, SongulOzdemir, Hasan2026-03-262026-03-2620222365-654910.1002/slct.2022006572-s2.0-85134514231https://doi.org/10.1002/slct.202200657https://hdl.handle.net/20.500.14901/1842Gerni, Serpil/0000-0001-7699-1697; Korkmaz, Işıl Nihan/0000-0003-4896-5226; Bayrak, Songül/0000-0001-6424-2760In this study, a new affinity process was developed for the purification of Lactoperoxidase with synthesized sixteen aminobenzohydrazide derivatives. For this purpose, ligands were covalently bound to CNBr-activated Sepharose-4B-L-tyrosine matrix and affinity columns were prepared, and LPO was purified in one step with high yield and purity. Among all synthesized molecules, the 4-amino-3-bromo-2-methylbenzohydrazide molecule had a high usable potential in the purification of Lactoperoxidase from mammalian milk. Lactoperoxidase was purified 411.8 times with a yield of 17.38 % from goat milk, 187.25 times with a yield of 9.72 % buffalo milk, 2772.4 times with a yield of 18.98 % from bovine milk, and 1246.65 times with a yield of 4.43 % from sheep milk. It was demonstrated for the first time that aminobenzohydrazide molecules could be used as ligands in the purification of Lactoperoxidase enzyme.eninfo:eu-repo/semantics/closedAccessAffinity ChromatographyAminobenzohidrazideLactoperoxidaseMammalian MilkPurificationArticle