Highly active horseradish peroxidase immobilized in 1-butyl-3-methylimidazolium tetrafluoroborate room-temperature ionic liquid based sol-gel host materials.
Dramatically enhanced activity and excellent thermal stability of horseradish peroxidase were obtained by immobilizing it in a 1-butyl-3-methylimidazolium tetrafluoroborate room-temperature ionic liquid based sol-gel matrix.
Liu
Yang
Y
State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, China.
Wang
Meijia
M
Li
Jun
J
Li
Zhiying
Z
He
Ping
P
Liu
Hongtao
H
Li
Jinghong
J
D001881:Borates / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007093:Imidazoles / Q000737:chemistry*; D007477:Ions / Q000737:chemistry; D007700:Kinetics; D046529:Microscopy, Electron, Transmission; D044367:Phase Transition; D013696:Temperature
C419324:1-butyl-3-methylimidazolium tetrafluoroborate; D001881:Borates; D004800:Enzymes, Immobilized; D007093:Imidazoles; D007477:Ions; D006735:Horseradish Peroxidase