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Article 2022 · 7 citations

A New Affinity Matrixe Synthesized from Aminobenzohydrazide Derivatives for Purification of Lactoperoxidase Enzyme

Kavaz, Neslihan Macit, Erel, Deniz, Korkmaz, Isil Nihan, Gerni, Serpil, Abul, Nurgul, Bayrak, Songul, Koksal, Zeynep, Kalin, Ramazan, Oztekin, Aykut, Ozdemir, Hasan

Abstract

In 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.

Keywords
Affinity chromatography aminobenzohidrazide lactoperoxidase mammalian milk purification GLUTATHIONE-S-TRANSFERASE STEP PURIFICATION BOVINE-MILK BUTYRYLCHOLINESTERASE ACETYLCHOLINESTERASE PEROXIDASE INHIBITION PROTEINS SYSTEM
WoS Categories
Chemistry, Multidisciplinary
Sustainable Development Goals
Citation
Journal
CHEMISTRYSELECT
Year
2022
Volume
7
Issue
27
ISSN
2365-6549
DOI
10.1002/slct.202200657
WoS UID
WOS:000825281500001
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