Partition of horseradish peroxidase with maintained activity in aqueous biphasic system based on ionic liquid

Enzyme activity and partition behavior in aqueous biphasic systems (ABSs) consisting of ionic liquid (IL) and salt (IL-ABSs) were investigated to increase our understanding of IL-ABSs and shed light on their application potential as enzyme extraction system. With horseradish peroxidase (HRP) as the...

Full description

Bibliographic Details
Published in:Talanta
Main Authors: Cao, Qing, Quan, Li, He, Chiyang, Li, Na, Li, Kean, Liu, Feng
Other Authors: Liu, F (reprint author), Peking Univ, Coll Chem, Minist Educ,Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Chengfu Rd, Beijing 100871, Peoples R China., Peking Univ, Coll Chem, Minist Educ,Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Beijing 100871, Peoples R China., Anqing Normal Coll, Dept Chem, Anqing 246011, Peoples R China., Peking Univ, Coll Chem, Minist Educ,Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Chengfu Rd, Beijing 100871, Peoples R China.
Format: Journal/Newspaper
Language:English
Published: talanta 2008
Subjects:
Online Access:https://hdl.handle.net/20.500.11897/197785
https://doi.org/10.1016/j.talanta.2008.05.055
id ftpekinguniv:oai:localhost:20.500.11897/197785
record_format openpolar
spelling ftpekinguniv:oai:localhost:20.500.11897/197785 2023-05-15T13:50:36+02:00 Partition of horseradish peroxidase with maintained activity in aqueous biphasic system based on ionic liquid Cao, Qing Quan, Li He, Chiyang Li, Na Li, Kean Liu, Feng Liu, F (reprint author), Peking Univ, Coll Chem, Minist Educ,Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Chengfu Rd, Beijing 100871, Peoples R China. Peking Univ, Coll Chem, Minist Educ,Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Beijing 100871, Peoples R China. Anqing Normal Coll, Dept Chem, Anqing 246011, Peoples R China. Peking Univ, Coll Chem, Minist Educ,Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Chengfu Rd, Beijing 100871, Peoples R China. 2008 https://hdl.handle.net/20.500.11897/197785 https://doi.org/10.1016/j.talanta.2008.05.055 en eng talanta TALANTA.2008,77,(1),160-165. 672253 0039-9140 http://hdl.handle.net/20.500.11897/197785 doi:10.1016/j.talanta.2008.05.055 18804614 WOS:000260290200024 PubMed EI SCI Horseradish peroxidase Enzyme activity Partition Ionic liquid Aqueous biphasic system ANTARCTICA LIPASE-B 2-PHASE SYSTEM SOLVENT-EXTRACTION CROWN-ETHER SEPARATION WATER SALT SELECTIVITY STABILITY MEDIA Journal 2008 ftpekinguniv https://doi.org/20.500.11897/197785 https://doi.org/10.1016/j.talanta.2008.05.055 2021-08-01T08:25:24Z Enzyme activity and partition behavior in aqueous biphasic systems (ABSs) consisting of ionic liquid (IL) and salt (IL-ABSs) were investigated to increase our understanding of IL-ABSs and shed light on their application potential as enzyme extraction system. With horseradish peroxidase (HRP) as the model enzyme, several effects of alkylimidazolium chloride-K2HPO4 ABSs on activity and partition behavior of enzyme were studied including alkyl chain length of ILs and concentrations of each component. High lyotropic ILs (1-butyl-3-methylimidazolium and 1-ethyl-3-methylimidazolium chloride) and adequate water content (>40%) were both essential for the activity maintenance of HRP in IL-ABS. 1-Butyl-3-methylimidazolium chloride ([C(4)mim]Cl) was found to be an appropriate IL for phase forming and HRP activity retaining. After optimization of phase condition, about 80% HRP amount was distributed in the IL-rich upper phase, and greater than 90% enzyme activity was obtained. Moreover, compared with the commonly used polymer-based ABSs, this [C(4)mim]Cl-ABS has a much lower viscosity, which is very beneficial to the experimental operation. Therefore, the tested IL-ABS could be considered as a potential enzyme extraction system. (C) 2008 Elsevier B.V. All rights reserved. Chemistry, Analytical SCI(E) EI PubMed 30 ARTICLE 1 160-165 77 Journal/Newspaper Antarc* Antarctica Peking University Institutional Repository (PKU IR) Talanta 77 1 160 165
institution Open Polar
collection Peking University Institutional Repository (PKU IR)
op_collection_id ftpekinguniv
language English
topic Horseradish peroxidase
Enzyme activity
Partition
Ionic liquid
Aqueous biphasic system
ANTARCTICA LIPASE-B
2-PHASE SYSTEM
SOLVENT-EXTRACTION
CROWN-ETHER
SEPARATION
WATER
SALT
SELECTIVITY
STABILITY
MEDIA
spellingShingle Horseradish peroxidase
Enzyme activity
Partition
Ionic liquid
Aqueous biphasic system
ANTARCTICA LIPASE-B
2-PHASE SYSTEM
SOLVENT-EXTRACTION
CROWN-ETHER
SEPARATION
WATER
SALT
SELECTIVITY
STABILITY
MEDIA
Cao, Qing
Quan, Li
He, Chiyang
Li, Na
Li, Kean
Liu, Feng
Partition of horseradish peroxidase with maintained activity in aqueous biphasic system based on ionic liquid
topic_facet Horseradish peroxidase
Enzyme activity
Partition
Ionic liquid
Aqueous biphasic system
ANTARCTICA LIPASE-B
2-PHASE SYSTEM
SOLVENT-EXTRACTION
CROWN-ETHER
SEPARATION
WATER
SALT
SELECTIVITY
STABILITY
MEDIA
description Enzyme activity and partition behavior in aqueous biphasic systems (ABSs) consisting of ionic liquid (IL) and salt (IL-ABSs) were investigated to increase our understanding of IL-ABSs and shed light on their application potential as enzyme extraction system. With horseradish peroxidase (HRP) as the model enzyme, several effects of alkylimidazolium chloride-K2HPO4 ABSs on activity and partition behavior of enzyme were studied including alkyl chain length of ILs and concentrations of each component. High lyotropic ILs (1-butyl-3-methylimidazolium and 1-ethyl-3-methylimidazolium chloride) and adequate water content (>40%) were both essential for the activity maintenance of HRP in IL-ABS. 1-Butyl-3-methylimidazolium chloride ([C(4)mim]Cl) was found to be an appropriate IL for phase forming and HRP activity retaining. After optimization of phase condition, about 80% HRP amount was distributed in the IL-rich upper phase, and greater than 90% enzyme activity was obtained. Moreover, compared with the commonly used polymer-based ABSs, this [C(4)mim]Cl-ABS has a much lower viscosity, which is very beneficial to the experimental operation. Therefore, the tested IL-ABS could be considered as a potential enzyme extraction system. (C) 2008 Elsevier B.V. All rights reserved. Chemistry, Analytical SCI(E) EI PubMed 30 ARTICLE 1 160-165 77
author2 Liu, F (reprint author), Peking Univ, Coll Chem, Minist Educ,Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Chengfu Rd, Beijing 100871, Peoples R China.
Peking Univ, Coll Chem, Minist Educ,Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Beijing 100871, Peoples R China.
Anqing Normal Coll, Dept Chem, Anqing 246011, Peoples R China.
Peking Univ, Coll Chem, Minist Educ,Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Chengfu Rd, Beijing 100871, Peoples R China.
format Journal/Newspaper
author Cao, Qing
Quan, Li
He, Chiyang
Li, Na
Li, Kean
Liu, Feng
author_facet Cao, Qing
Quan, Li
He, Chiyang
Li, Na
Li, Kean
Liu, Feng
author_sort Cao, Qing
title Partition of horseradish peroxidase with maintained activity in aqueous biphasic system based on ionic liquid
title_short Partition of horseradish peroxidase with maintained activity in aqueous biphasic system based on ionic liquid
title_full Partition of horseradish peroxidase with maintained activity in aqueous biphasic system based on ionic liquid
title_fullStr Partition of horseradish peroxidase with maintained activity in aqueous biphasic system based on ionic liquid
title_full_unstemmed Partition of horseradish peroxidase with maintained activity in aqueous biphasic system based on ionic liquid
title_sort partition of horseradish peroxidase with maintained activity in aqueous biphasic system based on ionic liquid
publisher talanta
publishDate 2008
url https://hdl.handle.net/20.500.11897/197785
https://doi.org/10.1016/j.talanta.2008.05.055
genre Antarc*
Antarctica
genre_facet Antarc*
Antarctica
op_source PubMed
EI
SCI
op_relation TALANTA.2008,77,(1),160-165.
672253
0039-9140
http://hdl.handle.net/20.500.11897/197785
doi:10.1016/j.talanta.2008.05.055
18804614
WOS:000260290200024
op_doi https://doi.org/20.500.11897/197785
https://doi.org/10.1016/j.talanta.2008.05.055
container_title Talanta
container_volume 77
container_issue 1
container_start_page 160
op_container_end_page 165
_version_ 1766253753402392576