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    Home > Biochemistry News > Biotechnology News > Wuhan Institute of Virology/Biosafety Science Center-Institute of Biophysics joint team has made new progress in the precise construction of highly efficient organic phase catalytic nanostructures

    Wuhan Institute of Virology/Biosafety Science Center-Institute of Biophysics joint team has made new progress in the precise construction of highly efficient organic phase catalytic nanostructures

    • Last Update: 2022-01-10
    • Source: Internet
    • Author: User
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    Recently, the international academic journal
    ACS Catalysis ("ACS Catalysis") published online the latest research results of the joint team of the Mendong research group of the Wuhan Institute of Virology of the Chinese Academy of Sciences/the University of Biosafety Science Research Center and the Zhang Xianen research group of the Institute of Biophysics of the Chinese Academy of Sciences
    .
    The paper is entitled "Self-assembled enzymatic nanowires with a'dry and wet' interface improve the catalytic performance of Januvia transaminase in organic solvent"

    .
    The research developed a self-assembled enzyme nanowire with a unique "dry and wet" interface (hydrophobic-hydrophilic hybrid interface), which can effectively improve the catalytic performance of transaminase in organic solvents

    .


    Enzymatic catalysis is considered to be one of the main driving forces of the chemical industry.
    Enzyme molecules have a variety of desirable properties and have a wide range of applications, from the synthesis of pharmaceutical intermediates to the large-scale use of renewable resources to produce biofuels

    .
    However, many prodrugs as reaction substrates cannot be dissolved in water and need to be reacted in organic solvents

    .
    Although there are many advantages to enzymatically catalyzed reactions in organic solvents, organic solvents usually cause the denaturation of enzyme molecules, thereby affecting its catalytic performance

    .
    Therefore, improving the stability of enzyme molecules in organic solvents is the key to improving the catalytic performance of the enzyme in the organic phase

    .


    In response to the above problems, this study used the properties of yeast prion protein Sup35 to self-assemble to form linear nanostructures,
    and fused
    Januvia aminotransferase (JTA), a key enzyme in the synthesis of sitagliptin (diabetes treatment drug) , with the Sup35 self-assembly domain
    .
    Through the self-assembly of Sup35, JTA demonstrated that JTA nanowires were formed on the surface of Sup35 nanowires

    .
    Enzyme molecules interact with nanowires to form a "dry and wet" hybrid interface with both hydrophilic and hydrophobic properties.
    On the one hand, the interface enriches hydrophobic substrate molecules through the hydrophobic microenvironment on the surface, and on the other The hydrophilic part of the surface protects the stability of JTA in organic solvents, thereby improving the catalytic performance of JTA in organic solvents

    .
    The catalytic activity of the obtained JTA nanowires ((33.
    610±2.
    406)×10
    -3 s -1 ) is more than 4.
    7 times higher than that of
    free JTA ((7.
    088±0.
    351)×10
    -3 s -1 ), and the conversion rate is 90% The required time is shortened from 24h for free JTA to less than 4.
    5h

    .
    JTA nanowires show better thermal stability and pH stability than free JTA, as well as better organic solvent adaptability

    .
    This self-assembly strategy provides a promising technical route for improving the performance of enzymes in organic solvents

    .


    Wei Cuihua, a doctoral student at the Wuhan Institute of Virology, is the first author of the paper, a researcher from the Wuhan Institute of Virology Aston and a researcher from the Institute of Biophysics Zhang Xianen are the co-corresponding authors of the paper

    .
    This research was funded by the National Natural Science Foundation of China, the National Key Research and Development Program, the Strategic Key Research Program of the Chinese Academy of Sciences, and the Youth Promotion Association of the Chinese Academy of Sciences

    .


    Article link:
    https://pubs.
    acs.
    org/doi/10.
    1021/acscatal.
    1c04293

     

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