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Carboxyethyl-functionalized 3D porous polypyrrole synthesized using a porogen-free method for covalent immobilization of urease

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22310%2F21%3A43922845" target="_blank" >RIV/60461373:22310/21:43922845 - isvavai.cz</a>

  • Alternative codes found

    RIV/60461373:22310/20:43921851 RIV/60461373:22330/20:43921851 RIV/60461373:22340/20:43921851 RIV/60461373:22330/21:43922845 RIV/60461373:22340/21:43922845

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S1387181120306909?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S1387181120306909?via%3Dihub</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.micromeso.2020.110690" target="_blank" >10.1016/j.micromeso.2020.110690</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Carboxyethyl-functionalized 3D porous polypyrrole synthesized using a porogen-free method for covalent immobilization of urease

  • Original language description

    The immobilization of enzymes onto porous supports is a common strategy for obtaining improved stability, fast product separation, enzyme reusability, and, ultimately, lower operating costs. Therefore, the development of new supports with specific surface functionalities that enable the covalent attachment of enzymes is of significant interest. Herein, stable three-dimensional (3D) porous materials were synthesized from polypyrrole by a simple template approach and used as an immobilization support for urease. The template method entails the use of polypyrrole nanoparticle building blocks, onto which a carboxylic acid-functionalized pyrrole monomer was polymerized, forming a 3D porous structure with tunable pore size distribution. Scanning electron microscopy (SEM) images, together with static light scattering (SLS), revealed the 3D porous nature of the materials. The properties of both the supports and the immobilized enzyme were characterized using a combination of techniques. The ability of the bioconjugated urease to catalyze the hydrolysis of urea into carbon dioxide and ammonia was then tested. The immobilized enzyme exhibited good catalytic activity, stability and reusability. Overall, these results suggest that such 3D porous materials with chemically accessible surfaces have considerable potential for use as biocatalyst supports.

  • 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

    20401 - Chemical engineering (plants, products)

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

    2021

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Microporous and mesoporous materials

  • ISSN

    1387-1811

  • e-ISSN

  • Volume of the periodical

    311

  • Issue of the periodical within the volume

    FEB 2021

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    11

  • Pages from-to

    110690

  • UT code for WoS article

    000600421100004

  • EID of the result in the Scopus database

    2-s2.0-85092784477