ArticleBMC chemistry2026
Immobilization and characterization of bovine carbonic anhydrase enzyme on iron oxide magnetic nanoparticles: investigation of potential applicability in CO
Article in BMC chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
In this study, carbonic anhydrase (CA) was purified from bovine erythrocytes using a Sepharose 4B-L-tyrosine sulfanilamide affinity chromatography method, achieving an 83.42-fold purification. The source of the enzyme is bovine blood erythrocytes, which were obtained from a slaughterhouse. Following purification, two different support materials (Fe₃O₄-NH₂ and Fe₃O₄@SiO₂-NH₂) were synthesized for enzyme immobilization, and sığır karbonik anhidraz (BCA) was immobilized via the covalent binding method. The support material prior to immobilisation and the enzyme-bound support material after immobilisation were characterised by FT-IR, SEM-EDX and VSM. The kinetic parameters of free BCA were determined as Km = 4.888 mM and Vmax = 3.081 µmol min
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