Organic Co-solvents Affect Activity, Stability and Enantioselectivity of Haloalkane Dehalogenases

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F13%3A00065823" target="_blank" >RIV/00216224:14310/13:00065823 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00159816:_____/13:00063741

Výsledek na webu

<a href="http://dx.doi.org/10.1002/biot.201200378" target="_blank" >http://dx.doi.org/10.1002/biot.201200378</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/biot.201200378" target="_blank" >10.1002/biot.201200378</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Organic Co-solvents Affect Activity, Stability and Enantioselectivity of Haloalkane Dehalogenases

Popis výsledku v původním jazyce

Haloalkane dehalogenases are microbial enzymes with a wide range of biotechnological applications. The use of organic co-solvents to solubilize their hydrophobic substrates is often necessary. In order to choose the most compatible co-solvent, the effects of fourteen co-solvents on activity, stability and enantioselectivity of three model enzymes, DbjA, DhaA and LinB, were evaluated. All co-solvents caused at high concentration loss of activity and conformational changes. The highest inactivation was induced by tetrahydrofuran, while more hydrophilic co-solvents, such as ethylene glycol and dimethyl sulfoxide, were more tolerated. The effects of co-solvents at low concentration were different for each enzyme-solvent pair. The increase in DbjA activitywas induced by the majority of organic co-solvents tested, while activities of DhaA and LinB decreased at comparable concentrations of the same co-solvent. Moreover, high increase of DbjA enantioselectivity was observed.

Název v anglickém jazyce

Organic Co-solvents Affect Activity, Stability and Enantioselectivity of Haloalkane Dehalogenases

Popis výsledku anglicky

Haloalkane dehalogenases are microbial enzymes with a wide range of biotechnological applications. The use of organic co-solvents to solubilize their hydrophobic substrates is often necessary. In order to choose the most compatible co-solvent, the effects of fourteen co-solvents on activity, stability and enantioselectivity of three model enzymes, DbjA, DhaA and LinB, were evaluated. All co-solvents caused at high concentration loss of activity and conformational changes. The highest inactivation was induced by tetrahydrofuran, while more hydrophilic co-solvents, such as ethylene glycol and dimethyl sulfoxide, were more tolerated. The effects of co-solvents at low concentration were different for each enzyme-solvent pair. The increase in DbjA activitywas induced by the majority of organic co-solvents tested, while activities of DhaA and LinB decreased at comparable concentrations of the same co-solvent. Moreover, high increase of DbjA enantioselectivity was observed.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Biotechnology Journal

ISSN

1860-6768

e-ISSN

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Svazek periodika

8

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

11

Strana od-do

719-729

Kód UT WoS článku

000320031900013

EID výsledku v databázi Scopus

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