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

The result's identifiers

  • Result code in 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>

  • Alternative codes found

    RIV/00159816:_____/13:00063741

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

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

Others

  • Publication year

    2013

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Biotechnology Journal

  • ISSN

    1860-6768

  • e-ISSN

  • Volume of the periodical

    8

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    11

  • Pages from-to

    719-729

  • UT code for WoS article

    000320031900013

  • EID of the result in the Scopus database