All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

Graphene oxide immobilized enzymes show high thermal and solvent stability

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F15%3A00443878" target="_blank" >RIV/61388963:_____/15:00443878 - isvavai.cz</a>

  • Alternative codes found

    RIV/60461373:22310/15:43899655

  • Result on the web

    <a href="http://pubs.rsc.org/en/content/articlepdf/2015/nr/c5nr00438a" target="_blank" >http://pubs.rsc.org/en/content/articlepdf/2015/nr/c5nr00438a</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1039/c5nr00438a" target="_blank" >10.1039/c5nr00438a</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Graphene oxide immobilized enzymes show high thermal and solvent stability

  • Original language description

    The thermal and solvent tolerance of enzymes is highly important for their industrial use. We show here that the enzyme lipase from Rhizopus oryzae exhibits exceptionally high thermal stability and high solvent tolerance and even increased activity in acetone when immobilized onto a graphene oxide (GO) nanosupport prepared by Staudenmaier and Brodie methods. We studied various forms of immobilization of the enzyme: by physical adsorption, covalent attachment, and additional crosslinking. The activity recovery was shown to be dependent on the support type, enzyme loading and immobilization procedure. Covalently immobilized lipase showed significantly better resistance to heat inactivation (the activity recovery was 65% at 70 degrees C) in comparison with the soluble counterpart (the activity recovery was 65% at 40 degrees C). Physically adsorbed lipase achieved over 100% of the initial activity in a series of organic solvents. These findings, showing enhanced thermal stability and solve

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    CC - Organic chemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GA15-09001S" target="_blank" >GA15-09001S: Chemical modifications of graphene based materials: Synthesis of graphane and halogengraphene</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nanoscale

  • ISSN

    2040-3364

  • e-ISSN

  • Volume of the periodical

    7

  • Issue of the periodical within the volume

    13

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    7

  • Pages from-to

    5852-5858

  • UT code for WoS article

    000351619600036

  • EID of the result in the Scopus database

    2-s2.0-84925326333