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An automated method to evaluate the enzyme kinetics of β-glucosidases

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F17%3A43912527" target="_blank" >RIV/62156489:43210/17:43912527 - isvavai.cz</a>

  • Alternative codes found

    RIV/68081707:_____/17:00506682

  • Result on the web

    <a href="http://dx.doi.org/10.1002/pro.3078" target="_blank" >http://dx.doi.org/10.1002/pro.3078</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/pro.3078" target="_blank" >10.1002/pro.3078</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    An automated method to evaluate the enzyme kinetics of β-glucosidases

  • Original language description

    Enzyme kinetic measurements are important for the characterization and engineering of biocatalysts, with applications in a wide range of research fields. The measurement of initial reaction velocity is usually slow and laborious, which motivated us to explore the possibilities for automating this process. Our model enzyme is the maize β-glucosidase Zm-p60.1. Zm-p60.1 plays a significant role in plant growth and development by regulating levels of the active plant hormone cytokinin. Zm-p60.1 belongs to a wide group of hydrolytic enzymes. Members of this group hydrolyze several different types of glucosides, releasing glucose as a secondary product. Enzyme kinetic measurements using artificial substrates are well established, but burdensome and time-consuming. Thus, they are a suitable target for process automation. Simple optical methods for enzyme kinetic measurements using natural substrates are often impossible given the optical properties of the enzymatic reaction products. However, we have developed an automated method based on glucose detection, as glucose is released from all substrates of glucosidase reactions. The presented method can obtain 24 data points from up to 15 substrate concentrations to precisely describe the enzyme kinetics. The combination of an automated liquid handling process with assays that have been optimized for measuring the initial hydrolysis velocity of β-glucosidases yields two distinct methods that are faster, cheaper, and more accurate than the established protocols.

  • 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

    10609 - Biochemical research methods

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

    2017

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Protein Science

  • ISSN

    0961-8368

  • e-ISSN

  • Volume of the periodical

    26

  • Issue of the periodical within the volume

    2

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    7

  • Pages from-to

    382-388

  • UT code for WoS article

    000393960300021

  • EID of the result in the Scopus database

    2-s2.0-85005931258