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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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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