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Laccase and horseradish peroxidase for green treatment of phenolic micropollutants in real drinking water and wastewater

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F21%3A00544749" target="_blank" >RIV/61388971:_____/21:00544749 - isvavai.cz</a>

  • Alternative codes found

    RIV/46747885:24220/21:00008428 RIV/46747885:24620/21:00008428 RIV/00216208:11310/21:10430084

  • Result on the web

    <a href="https://link.springer.com/article/10.1007%2Fs11356-021-12910-0" target="_blank" >https://link.springer.com/article/10.1007%2Fs11356-021-12910-0</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s11356-021-12910-0" target="_blank" >10.1007/s11356-021-12910-0</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Laccase and horseradish peroxidase for green treatment of phenolic micropollutants in real drinking water and wastewater

  • Original language description

    Biologically active micropollutants that contain diverse phenolic/aromatic structures are regularly present in wastewater effluents and are even found in drinking water. Advanced green technologies utilizing immobilized laccase and/or peroxidase, which target these micropollutants directly, may provide a reasonable alternative to standard treatments. Nevertheless, the use of these enzymes is associated with several issues that may prevent their application, such as the low activity of laccase at neutral and basic pH or the necessity of hydrogen peroxide addition as a co-substrate for peroxidases. In this study, the activity of laccase from Trametes versicolor and horseradish peroxidase was evaluated across a range of commonly used substrates (2,2 '-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS), syringaldazine, and guaiacol). Moreover, conditions for their optimal performance were explored along with an assessment of whether these conditions accurately reflect the effectivity of both enzymes in the degradation of a mixture of bisphenol A, 17 alpha-ethinylestradiol, triclosan, and diclofenac in tap drinking water and secondary wastewater effluent. Laccase and horseradish peroxidase showed optimal activity at strongly acidic pH if ABTS was used as a substrate. Correspondingly, the activities of both enzymes detected using ABTS in real waters were significantly enhanced by adding approximately 2.5% (v/v) of McIlvaine's buffer. Degradation of a mixture of micropollutants in wastewater with 2.5% McIlvaine's buffer (pH 7) resulted in a substantial decrease in estrogenic activity. Low degradation efficiency of micropollutants by laccase was observed in pure McIlvaine's buffer of pH 3 and 7, compared with efficient degradation in tap water of pH 7.5 without buffer.

  • 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

    20801 - Environmental biotechnology

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

    Environmental Science and Pollution Research

  • ISSN

    0944-1344

  • e-ISSN

    1614-7499

  • Volume of the periodical

    28

  • Issue of the periodical within the volume

    24

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    9

  • Pages from-to

    31566-31574

  • UT code for WoS article

    000619737500021

  • EID of the result in the Scopus database

    2-s2.0-85101199373