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Title:Ionic liquids as (co)solvents for enzymatic reactions
Authors:ID Paljevac, Muzafera (Author)
ID Leitgeb, Maja (Author)
ID Knez, Željko (Author)
Files:.pdf Chemical_Industry_and_Chemical_Engineering_Quarterly_2006_Paljevac,_Habulin,_Knez_Ionic_liquids_as_(co)solvents_for_enzymatic_reactions.pdf (360,03 KB)
MD5: 4F495A1F799D29FAEAAFD9A0CB74FBFC
PID: 20.500.12556/dkum/d604a8ac-8c5d-460c-b6df-fe57fa53cff3
 
URL http://www.doiserbia.nb.rs/Article.aspx?id=1451-93720603181P
 
Language:English
Work type:Scientific work
Typology:1.01 - Original Scientific Article
Organization:FKKT - Faculty of Chemistry and Chemical Engineering
Abstract:Ionic liquids are low melting point salts that represent an excitnq new class of reaction solvents. Many reactions show advantages when carried out in ionic liquids, either with regard to enhanced reaction rates, improved selectivity, or easier reuse of catalysts. To ascertain the influence of ionic liquids on the enzyme activity three different ionic liquids, 1-butyl-3-methylimidazolium chloride ([bmim] [Cl]), 1-butyl-3-methylimidazolium hexafluorophosphate ([bmim] [PF6]) and 1-butyl-3-methylimidazolium tetrafluoroborate ([bmim][BF4]) were synthesized and investigated as potential media for the hydrolysis of carboxymethyl cellulose, catalyzed by non-immobilized cellulase from Humicola insolens (Celluzyme 0,7T) and for ester synthesis, catalyzed by immobilized lipase from Rhyomucor miehei (Lipozyme RM IM). Enzyme-catalyzed reactions were performed in a batch stirred reactor at atmospheric pressure. Celluzyme 0.7T showed better activity in hydrophobic ionic liquid ([bmim] [PF6]), as compared to hydrophilic ionic liquid ([bmim] [BF4]). In the case of Lipozyme RM IM, the synthetic activity of the enzyme was strongly reduced by incubating the enzyme in ionic liquids. Paper presented at the 1st South-East European congress of chemical engineering, Belgrade, September 25-28, 2005
Keywords:chemical processing, ion liquids, organic salts, biotechnology, enzymatic catalysis, immobilized lipase stability
Publication status:Published
Publication version:Version of Record
Year of publishing:2006
Number of pages:str. 181-186
Numbering:Letn. 12, št. 3
PID:20.500.12556/DKUM-25758 New window
ISSN:1451-9372
UDC:66.097
ISSN on article:1451-9372
COBISS.SI-ID:10667542 New window
DOI:10.2298/CICEQ0603181P New window
NUK URN:URN:SI:UM:DK:FENCTRNW
Publication date in DKUM:31.05.2012
Views:2434
Downloads:369
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Categories:Misc.
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Record is a part of a journal

Title:Chemical Industry & Chemical Engineering Quarterly
Shortened title:Chem. Ind. Chem. Eng. Q.
Publisher:Savez hemijskih inženjera Srbije
ISSN:1451-9372
COBISS.SI-ID:9527830 New window

Licences

License:CC BY-NC-ND 4.0, Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
Link:http://creativecommons.org/licenses/by-nc-nd/4.0/
Description:The most restrictive Creative Commons license. This only allows people to download and share the work for no commercial gain and for no other purposes.
Licensing start date:31.05.2012

Secondary language

Language:Serbian
Title:Jonske tečnosti kao ko-solventi za enzimske reakcije
Abstract:Jonske tečnosti imaju niske temperature mržnjenja i kao takve predstavljaju novu klasu rastvarača koji se mogu iskoristiti u mnogim reakcijama. Očigledne su prednosti kada se hemijska reakcija izvodi uz prisustvo jonskih tečnosti bilo kod ubrzanja brzine hemijske reakcije, povećane selektivnosti ili jednostavnije ponovne upotrebe katalizatora. U cilju utvrđivanja uticaja jonskih tečnosti na aktivnost enzima, sintetizovane su i ispitane tri različite tečnosti, l-butil-3-meilimidazolijum hlorid ([bmim][CI]) 1-butil-3-metilimidazolijum heksafluorofosfat ([bmim][PF6]) i 1-butil-3-metilimidazolijum tetrafluoroborat ([bmim][BF4]) kao potencijalni rastvarači u reakcijama hidrolize karboksimetil celuloze koja je katalizovana neimobilisanom celulazom iz Humicola insolens (Celluzyme 0,7T) i sintezama estara katalizovanim imobilisanom lipazom iz Rhizomucor miehei (Lipozvme RM IM). Enzimski katalizovane reakcije su izvedene u šaržnom reaktoru pod atmosferskim pritiskom. Pokazalo se da Celluzyme 0,7T ima veću aktivnost u hidrofobnoj jonskoj tečnosti [bmim][PF6]), u odnosu na hidrofilnu ([bmim][BF4]). U slučaju Lipozyme RM IM, aktivnost enzima je značajno smanjena inkubacijom enzima u jonskoj tečnosti.
Keywords:kemijska procesna tehnika, ionske raztopine, organske soli, biotehnologija, encimatska kataliza, stabilnost imobilizirane lipaze


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