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Advanced database mining of efficient haloalkane dehalogenases by sequence and structure bioinformatics and microfluidics

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F22%3A00077764" target="_blank" >RIV/00159816:_____/22:00077764 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216305:26230/22:PU147439 RIV/00216224:14310/22:00128314

  • Result on the web

    <a href="https://www.sciencedirect.com/science/article/abs/pii/S2667109322005036" target="_blank" >https://www.sciencedirect.com/science/article/abs/pii/S2667109322005036</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.checat.2022.09.011" target="_blank" >10.1016/j.checat.2022.09.011</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Advanced database mining of efficient haloalkane dehalogenases by sequence and structure bioinformatics and microfluidics

  • Original language description

    Next-generation sequencing doubles genomic databases every 2.5 years. The accumulation of sequence data provides a unique opportunity to identify interesting biocatalysts directly in the databases without tedious and time-consuming engineering. Herein, we present a pipeline integrating sequence and structural bioinformatics with microfluidic enzymology for bioprospecting of efficient and robust haloalkane dehalogenases. The bioinformatic part identified 2,905 putative dehalogenases and prioritized a &quot;small-but-smart&apos;&apos; set of 45 genes, yielding 40 active enzymes, 24 of which were biochemically characterized by microfluidic enzymology techniques. Combining microfluidics with modern global data analysis provided precious mechanistic insights related to the high catalytic efficiency of selected enzymes. Overall, we have doubled the dehalogenation &quot;toolbox&apos;&apos; characterized over three decades, yielding biocatalysts that surpass the efficiency of currently available wild-type and engineered enzymes. This pipeline is generally applicable to other enzyme families and can accelerate the identification of efficient biocatalysts for industrial use.

  • 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

    10403 - Physical chemistry

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

    2022

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    CHEM CATALYSIS

  • ISSN

    2667-1093

  • e-ISSN

  • Volume of the periodical

    2

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    22

  • Pages from-to

    2704-2725

  • UT code for WoS article

    000901460400007

  • EID of the result in the Scopus database