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Xylanase immobilization onto trichlorotriazine-functionalized polyethylene glycol grafted magnetic nanoparticles: A thermostable and robust nanobiocatalyst for fruit juice clarification

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F20%3A73603067" target="_blank" >RIV/61989592:15310/20:73603067 - isvavai.cz</a>

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/pii/S0141813020337272" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813020337272</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.ijbiomac.2020.06.273" target="_blank" >10.1016/j.ijbiomac.2020.06.273</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Xylanase immobilization onto trichlorotriazine-functionalized polyethylene glycol grafted magnetic nanoparticles: A thermostable and robust nanobiocatalyst for fruit juice clarification

  • Original language description

    The covalent immobilization of xylanase onto the trichlorotriazine-functionalized polyethylene glycol grafted magnetic nanoparticles was exploited to generate a stabilized xylanase with improved catalytic activity and stability. Several tools were deployed to monitor the synthesis and immobilization processes, the loading capacity of nanocarrier, and the structural/chemical characteristics of the nanobiocatalyst. The optimum immobilization yield of xylanase was 260 mg xylanase/g nanocarrier in 20 mM phosphate buffer, pH 6.5 at 25 degrees C. A forward shift in optimum pH (6.5 to 7.5) and temperature (60 to 70 degrees C) of xylanase was observed after immobilization and the performance of immobilized enzyme was improved at high temperatures and pHs as affirmed by enhancement of v(max) (2.69 to 6.01 U/mL) and decreases of E-a (14.61 to 13.41 kJ/mol). An increase in K-m from 25.51 to 40.42 mg/mL was recorded after immobilization. The obtained results indicated augmented thermal stability of the immobilized xylanase. Notably, it showed good reusability as validated by retention of 50% of its initial activity after nine recycles in enrichment of the pineapple juice clarification after 120 min incubation at 50 degrees C, pH 4.5. The structural analysis revealed some partial changes in the alpha-helix and beta-sheet content of the enzyme after several recycles.

  • 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

  • Continuities

    N - Vyzkumna aktivita podporovana z neverejnych zdroju

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

  • ISSN

    0141-8130

  • e-ISSN

  • Volume of the periodical

    163

  • Issue of the periodical within the volume

    NOV

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    12

  • Pages from-to

    402-413

  • UT code for WoS article

    000579839600042

  • EID of the result in the Scopus database

    2-s2.0-85088863211