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IMMOBILIZATION OF HORSERADISH PEROXIDASE: EFFECT OF THE SUPPORT AND THE DESIGN
Abstract
The magnetically recoverable biocatalyst was developed. The catalyst support is based on magnetite particles (MPs) composed of magnetite particles and coated with the amino terminated silica layer to facilitate further functionalization. This functionalization involves the attachment of the glutaraldehyde linker followed by the covalent attachment of horseradish peroxidase (HRP) via its amino groups. The catalyst was tested in the reaction of 2,3,6-trimethylphenol (TMP) oxidation to 2,3,5-trimethylhydrochinone (TMHQ), which is semi-product of vitamin E. Synthesized biocatalyst was characterized by TEM, IR spectroscopy, the study of magnetic characteristics was carried out with vibration magnetometer. The developed biocatalyst showed high activity in 2,3,6-trimethylphenol oxidation to 2,3,5-trimethylhydrochinone. The enzymes immobilization on the magnetic nanoparticles is a prospective way for obtaining highly effective, stable and easy separable biocatalysts.
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