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Design and development of spectrophotometric enzymatic cyanide assays

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F25%3A00605222" target="_blank" >RIV/61388971:_____/25:00605222 - isvavai.cz</a>

  • Alternative codes found

    RIV/68407700:21460/25:00382235 RIV/00216208:11310/25:10495585

  • Result on the web

    <a href="https://link.springer.com/article/10.1007/s00216-024-05703-0" target="_blank" >https://link.springer.com/article/10.1007/s00216-024-05703-0</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s00216-024-05703-0" target="_blank" >10.1007/s00216-024-05703-0</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Design and development of spectrophotometric enzymatic cyanide assays

  • Original language description

    Determination of free cyanide (fCN) is required for various industrial, environmental, food, and clinical samples. Enzymatic methods are not widely used in this field despite their selectivity and mild conditions. Therefore, we present here a proof of concept for new spectrophotometric enzymatic assays of fCN. These are based on the hydrolysis of fCN affording the readily detectable NADH. fCN is hydrolyzed either in one step by cyanide dihydratase (CynD) or in two steps by cyanide hydratase (CynH) and formamidase (AmiF). An advantage of the latter route is the higher activity of CynH and AmiF compared to CynD. In both cases, the resulting formate is then transformed by an NAD-dependent formate dehydrogenase (FDH). The NADH thus formed is quantified colorimetrically using a known method based on a reduction of a tetrazolium salt (WST-8) with NADH. The developed assays of fCN are selective except for formic acid interference, proceed under mild conditions, and, moreover, fCN is detoxified during the reactions. The assays proceeded in a microtiter plate format. The limit of detection (LOD) and the limit of quantification (LOQ) were lower for the three-enzyme (CynH-AmiF-FDH) method (7.00 and 21.2 mu mol/L, respectively) than for the two-enzyme (CynD-FDH) method (10.7 and 32.4 mu mol/L, respectively). In conclusion, the new fCN assays presented in this work are selective, high-throughput, do not require harsh conditions, and use only small amounts of chemicals and enzymes.

  • 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

    10406 - Analytical chemistry

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2025

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Analytical and Bioanalytical Chemistry

  • ISSN

    1618-2642

  • e-ISSN

    1618-2650

  • Volume of the periodical

    417

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    DE - GERMANY

  • Number of pages

    8

  • Pages from-to

    697-704

  • UT code for WoS article

    001380457600001

  • EID of the result in the Scopus database

    2-s2.0-85212503990