Comparison of catalysis by haloalkane dehalogenases in aqueous solutions of deep eutectic and organic solvents

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F14%3A00063737" target="_blank" >RIV/00159816:_____/14:00063737 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1039/c4gc00117f" target="_blank" >http://dx.doi.org/10.1039/c4gc00117f</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c4gc00117f" target="_blank" >10.1039/c4gc00117f</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Comparison of catalysis by haloalkane dehalogenases in aqueous solutions of deep eutectic and organic solvents

Popis výsledku v původním jazyce

Haloalkane dehalogenases catalyze the hydrolytic cleavage of carbon-halogen bonds in diverse halogenated hydrocarbons and are attractive catalysts for sustainable biotechnologies. However, their use in industrial processes is limited due to the poor water solubility of their substrates and the tendency of the substrates to undergo abiotic hydrolysis. Here we systematically and critically compare the performance of three haloalkane dehalogenases, DbjA, DhaA and LinB, in aqueous solutions of the deep eutectic solvent ethaline, its components (ethylene glycol and choline chloride), and two organic solvents (methanol and acetone). Each of the solvents had different effects on the activity of each enzyme. Haloalkane dehalogenase DhaA was found to be the most tolerant to ethaline, retaining 21% of its reference activity even in solutions containing 90% (v/v) of ethaline. However, dissolution in 75% (v/v) ethylene glycol, 50% (v/v) methanol, or 25% (v/v) acetone caused almost total loss of Dh

Název v anglickém jazyce

Comparison of catalysis by haloalkane dehalogenases in aqueous solutions of deep eutectic and organic solvents

Popis výsledku anglicky

Haloalkane dehalogenases catalyze the hydrolytic cleavage of carbon-halogen bonds in diverse halogenated hydrocarbons and are attractive catalysts for sustainable biotechnologies. However, their use in industrial processes is limited due to the poor water solubility of their substrates and the tendency of the substrates to undergo abiotic hydrolysis. Here we systematically and critically compare the performance of three haloalkane dehalogenases, DbjA, DhaA and LinB, in aqueous solutions of the deep eutectic solvent ethaline, its components (ethylene glycol and choline chloride), and two organic solvents (methanol and acetone). Each of the solvents had different effects on the activity of each enzyme. Haloalkane dehalogenase DhaA was found to be the most tolerant to ethaline, retaining 21% of its reference activity even in solutions containing 90% (v/v) of ethaline. However, dissolution in 75% (v/v) ethylene glycol, 50% (v/v) methanol, or 25% (v/v) acetone caused almost total loss of Dh

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ED1.100%2F02%2F0123" target="_blank" >ED1.100/02/0123: Fakultní nemocnice u sv. Anny v Brně - Mezinárodní centrum klinického výzkumu (FNUSA - ICRC)</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Green Chemistry

ISSN

1463-9262

e-ISSN

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Svazek periodika

16

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

2754-2761

Kód UT WoS článku

000335005200049

EID výsledku v databázi Scopus

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