Peer-reviewed articles 17,970 +



Title: IMMOBILIZATION OF HORSERADISH PEROXIDASE: EFFECT OF THE SUPPORT AND THE DESIGN

IMMOBILIZATION OF HORSERADISH PEROXIDASE: EFFECT OF THE SUPPORT AND THE DESIGN
V. Matveeva;A. Sulman;B. Tikhonov;P. Stodolnikova;A. Sidorov
1314-2704
English
18
6.2
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.
conference
18th International Multidisciplinary Scientific GeoConference SGEM 2018
18th International Multidisciplinary Scientific GeoConference SGEM 2018, 02-08 July, 2018
Proceedings Paper
STEF92 Technology
International Multidisciplinary Scientific GeoConference-SGEM
Bulgarian Acad Sci; Acad Sci Czech Republ; Latvian Acad Sci; Polish Acad Sci; Russian Acad Sci; Serbian Acad Sci & Arts; Slovak Acad Sci; Natl Acad Sci Ukraine; Natl Acad Sci Armenia; Sci Council Japan; World Acad Sci; European Acad Sci, Arts & Letters; Ac
229-236
02-08 July, 2018
website
cdrom
1878
peroxidase; immobilization; magnetic nanoparticles; 2;3;6-trimethylphenol; oxidation