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Surface Interaction of Ionic Liquids: Stabilization of Polyethylene Terephthalate-Degrading Enzymes in Solution

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F22%3A00553493" target="_blank" >RIV/61388971:_____/22:00553493 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12310/22:43904932

  • Result on the web

    <a href="https://www.mdpi.com/1420-3049/27/1/119" target="_blank" >https://www.mdpi.com/1420-3049/27/1/119</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/molecules27010119" target="_blank" >10.3390/molecules27010119</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Surface Interaction of Ionic Liquids: Stabilization of Polyethylene Terephthalate-Degrading Enzymes in Solution

  • Original language description

    The effect of aqueous solutions of selected ionic liquids solutions on Ideonella sakaiensis PETase with bis(2-hydroxyethyl) terephthalate (BHET) substrate were studied by means of molecular dynamics simulations in order to identify the possible effect of ionic liquids on the structure and dynamics of enzymatic Polyethylene terephthalate (PET) hydrolysis. The use of specific ionic liquids can potentially enhance the enzymatic hydrolyses of PET where these ionic liquids are known to partially dissolve PET. The aqueous solution of cholinium phosphate were found to have the smallest effect of the structure of PETase, and its interaction with (BHET) as substrate was comparable to that with the pure water. Thus, the cholinium phosphate was identified as possible candidate as ionic liquid co-solvent to study the enzymatic hydrolyses of PET.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GA21-15936S" target="_blank" >GA21-15936S: Effects of Macromolecular Crowding on Enzyme Structure and Kinetics</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Molecules

  • ISSN

    1420-3049

  • e-ISSN

    1420-3049

  • Volume of the periodical

    27

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    15

  • Pages from-to

    119

  • UT code for WoS article

    000741757300001

  • EID of the result in the Scopus database

    2-s2.0-85122071344