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Published on: November 8, 2019
Purification of bovine serum paraoxonase and its immobilization on Eupergit C 250 L by covalent attachment
Murat Sayın1, Ozen Ozensoy Guler
1Department of Chemistry, Science and Art Faculty, Balikesir University , Cagıs-Kampus, Balikesir , Turkey and.
Abstract:
Serum paraoxonase (PON1) is a high-density lipoprotein (HDL)-associated enzyme that protects lipoproteins, both low-density lipoprotein (LDL) and HDL, against oxidation, and is considered as an antioxidative/anti-inflammatory component of HDL. In this study, PON1 was purified from bovine serum by ammonium sulfate precipitation and hydrophobic interaction chromatography on sepharose-4B-l-tyrosine-1-napthylamine. It was then immobilized on an unmodified Eupergit® C 250 L support. The immobilized PON1 retained a high catalytic activity and showed increased thermal stability compared to the native enzyme.

