Highly active horseradish peroxidase immobilized in 1-butyl-3-methylimidazolium tetrafluoroborate room-temperature ionic liquid based sol-gel host materials

Yang Liu; Meijia Wang; Jun Li; Zhiying Li; Ping He; Hongtao Liu; Jinghong Li

doi:10.1039/b417680d

Highly active horseradish peroxidase immobilized in 1-butyl-3-methylimidazolium tetrafluoroborate room-temperature ionic liquid based sol-gel host materials

Chem Commun (Camb). 2005 Apr 7:(13):1778-80. doi: 10.1039/b417680d. Epub 2005 Feb 2.

Authors

Yang Liu¹, Meijia Wang, Jun Li, Zhiying Li, Ping He, Hongtao Liu, Jinghong Li

Affiliation

¹ State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, China.

PMID: 15791330
DOI: 10.1039/b417680d

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Borates / chemistry*
Enzymes, Immobilized / metabolism*
Horseradish Peroxidase / metabolism*
Imidazoles / chemistry*
Ions / chemistry
Kinetics
Microscopy, Electron, Transmission
Phase Transition*
Temperature*

Substances

1-butyl-3-methylimidazolium tetrafluoroborate
Borates
Enzymes, Immobilized
Imidazoles
Ions
Horseradish Peroxidase