FTIR-based L-asparaginase activity assay enables continuous measurements in optically dense media including blood plasma
Complex heterogeneous systems, such as micelles or blood plasma, represent a particularly challenging environment to measure the catalytic parameters of some enzymes, including l-asparaginase. Existing methods are strongly interfered by the presence of plasma proteins, amino acids, as well as other...
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| Published in: | Analytical biochemistry Vol. 598; p. 113694 |
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| Format: | Journal Article |
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| Abstract | Complex heterogeneous systems, such as micelles or blood plasma, represent a particularly challenging environment to measure the catalytic parameters of some enzymes, including l-asparaginase. Existing methods are strongly interfered by the presence of plasma proteins, amino acids, as well as other components of plasma. Here we show that FTIR spectroscopy enables continuous real-time measurement of catalytic activity of l-asparaginase, in native and in PEG-chitosan conjugated form, in aqueous solutions as well as in heterogeneous non-transparent multicomponent systems, including colloidal systems or blood plasma, with minimal or no sample preparation. The approach developed is potentially applicable to other enzymatic reactions where the spectroscopic properties of substrate and product do not allow direct measurement with absorption or fluorescence spectroscopy.
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•New method is developed to determine catalytic parameters of l-asparaginase using FTIR spectroscopy.•The new method works well in complex heterogeneous systems, including blood plasma and reversed micelles.•Using the new method we performed the first ever direct measurement of dimeric L-asparaginase activity. |
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| AbstractList | Complex heterogeneous systems, such as micelles or blood plasma, represent a particularly challenging environment to measure the catalytic parameters of some enzymes, including l-asparaginase. Existing methods are strongly interfered by the presence of plasma proteins, amino acids, as well as other components of plasma. Here we show that FTIR spectroscopy enables continuous real-time measurement of catalytic activity of l-asparaginase, in native and in PEG-chitosan conjugated form, in aqueous solutions as well as in heterogeneous non-transparent multicomponent systems, including colloidal systems or blood plasma, with minimal or no sample preparation. The approach developed is potentially applicable to other enzymatic reactions where the spectroscopic properties of substrate and product do not allow direct measurement with absorption or fluorescence spectroscopy. Complex heterogeneous systems, such as micelles or blood plasma, represent a particularly challenging environment to measure the catalytic parameters of some enzymes, including l-asparaginase. Existing methods are strongly interfered by the presence of plasma proteins, amino acids, as well as other components of plasma. Here we show that FTIR spectroscopy enables continuous real-time measurement of catalytic activity of l-asparaginase, in native and in PEG-chitosan conjugated form, in aqueous solutions as well as in heterogeneous non-transparent multicomponent systems, including colloidal systems or blood plasma, with minimal or no sample preparation. The approach developed is potentially applicable to other enzymatic reactions where the spectroscopic properties of substrate and product do not allow direct measurement with absorption or fluorescence spectroscopy. [Display omitted] •New method is developed to determine catalytic parameters of l-asparaginase using FTIR spectroscopy.•The new method works well in complex heterogeneous systems, including blood plasma and reversed micelles.•Using the new method we performed the first ever direct measurement of dimeric L-asparaginase activity. |
| ArticleNumber | 113694 |
| Author | Pokrovskaya, Marina V. Kudryashova, Elena V. Sokolov, Nikolay N. Alexandrova, Svetlana S. Vinogradov, Alexander A. |
| Author_xml | – sequence: 1 givenname: Elena V. surname: Kudryashova fullname: Kudryashova, Elena V. email: helena_koudriachova@hotmail.com organization: Faculty of Chemistry, M.V. Lomonosov Moscow State University, Moscow, 119991, Russia – sequence: 2 givenname: Marina V. surname: Pokrovskaya fullname: Pokrovskaya, Marina V. organization: Institute of Biomedical Chemistry RAS, Pogodinskaya Str., 10/8, Moscow, 119121, Russia – sequence: 3 givenname: Svetlana S. surname: Alexandrova fullname: Alexandrova, Svetlana S. organization: Institute of Biomedical Chemistry RAS, Pogodinskaya Str., 10/8, Moscow, 119121, Russia – sequence: 4 givenname: Alexander A. orcidid: 0000-0002-4355-3022 surname: Vinogradov fullname: Vinogradov, Alexander A. organization: Faculty of Physics at National Research University Higher School of Economics, 21/4 Staraya Basmannaya Str., Moscow, 101000, Russia – sequence: 5 givenname: Nikolay N. surname: Sokolov fullname: Sokolov, Nikolay N. organization: Institute of Biomedical Chemistry RAS, Pogodinskaya Str., 10/8, Moscow, 119121, Russia |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32217095$$D View this record in MEDLINE/PubMed |
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| Keywords | PEG-chitosan Reversed micelles Catalytic activity Oligomeric composition l-asparaginase FTIR spectroscopy Blood plasma |
| Language | English |
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| SubjectTerms | Asparaginase - analysis Asparaginase - metabolism Biocatalysis Blood plasma Catalytic activity Chitosan - chemistry FTIR spectroscopy Humans l-asparaginase Oligomeric composition Pectobacterium carotovorum - enzymology PEG-chitosan Polyethylene Glycols - chemistry Reversed micelles Spectroscopy, Fourier Transform Infrared |
| Title | FTIR-based L-asparaginase activity assay enables continuous measurements in optically dense media including blood plasma |
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