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Mechanisms of Chemical and Enzymatic Reactions

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 June 2024) | Viewed by 2228

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Faculty of Chemistry, Institute of Applied Radiation Chemistry, Lodz University of Technology, Lodz, Poland
Interests: isotope effects; mechanisms of chemical and enzymatic reactions; enzyme inhibition; isotopic fractionation; isotope-ratio mass spectrometry; computational chemistry
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Special Issue Information

Dear Colleagues,

A plethora of applications of chemical and biochemical molecules, ranging from the medical use of small molecule drugs through complicated bio-vaccines to material design, cannot be achieved without a deep understanding of the processes involved in their preparation and action. This can be achieved nowadays via both experimental as well as theoretical studies. In this Special Issue, we would like to focus on the latest developments in the area of studying (bio)reaction mechanisms. Consequently, we look forward to collecting original research reports, as well as reviews of recent progress and perspectives from experts in the field.

Prof. Dr. Piotr Paneth
Guest Editor

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Keywords

  • reaction mechanism
  • enzymatic catalysis
  • theoretical calculations
  • isotope effects
  • kinetics
  • (AI-enhanced) QSAR

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Published Papers (1 paper)

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Research

15 pages, 2912 KiB  
Article
Sequential Co-Immobilization of Enzymes on Magnetic Nanoparticles for Efficient l-Xylulose Production
by Sanjay K. S. Patel, Rahul K. Gupta, Karthikeyan K. Karuppanan, In-Won Kim and Jung-Kul Lee
Int. J. Mol. Sci. 2024, 25(5), 2746; https://doi.org/10.3390/ijms25052746 - 27 Feb 2024
Viewed by 1532
Abstract
Multi-enzymatic strategies have shown improvement in bioconversion during cofactor regeneration. In this study, purified l-arabinitol 4-dehydrogenase (LAD) and nicotinamide adenine dinucleotide oxidase (Nox) were immobilized via individual, mixed, and sequential co-immobilization approaches on magnetic nanoparticles, and were evaluated to enhance the conversion [...] Read more.
Multi-enzymatic strategies have shown improvement in bioconversion during cofactor regeneration. In this study, purified l-arabinitol 4-dehydrogenase (LAD) and nicotinamide adenine dinucleotide oxidase (Nox) were immobilized via individual, mixed, and sequential co-immobilization approaches on magnetic nanoparticles, and were evaluated to enhance the conversion of l-arabinitol to l-xylulose. Initially, the immobilization of LAD or Nox on the nanoparticles resulted in a maximum immobilization yield and relative activity of 91.4% and 98.8%, respectively. The immobilized enzymes showed better pH and temperature profiles than the corresponding free enzymes. Furthermore, co-immobilization of these enzymes via mixed and sequential methods resulted in high loadings of 114 and 122 mg/g of support, respectively. Sequential co-immobilization of these enzymes proved more beneficial for higher conversion than mixed co-immobilization because of better retaining Nox residual activity. Sequentially co-immobilized enzymes showed a high relative conversion yield with broader pH, temperature, and storage stability profiles than the controls, along with high reusability. To the best of our knowledge, this is the first report on the mixed or sequential co-immobilization of LAD and Nox on magnetic nanoparticles for l-xylulose production. This finding suggests that selecting a sequential co-immobilization strategy is more beneficial than using individual or mixed co-immobilized enzymes on magnetic nanoparticles for enhancing conversion applications. Full article
(This article belongs to the Special Issue Mechanisms of Chemical and Enzymatic Reactions)
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