Enzyme activity measurement via spectral evolution profiling and PARAFAC

Andreas Baum, Anne S. Meyer, Javier Lopez Garcia, Max Egebo, Per Waaben Hansen, Jørn Dalgaard Mikkelsen

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The recent advances in multi-way analysis provide new solutions to traditional enzyme activity assessment. In the present study enzyme activity has been determined by monitoring spectral changes of substrates and products in real time. The method relies on measurement of distinct spectral fingerprints of the reaction mixture at specific time points during the course of the whole enzyme catalyzed reaction and employs multi-way analysis to detect the spectral changes. The methodology is demonstrated by spectral evolution profiling of Fourier Transform Infrared (FTIR) spectral fingerprints using parallel factor analysis (PARAFAC) for pectin lyase, glucose oxidase, and a cellulase preparation.
Original languageEnglish
JournalAnalytica Chimica Acta
Pages (from-to)1-8
Publication statusPublished - 2013


  • Chemometrics
  • Fourier transform infrared spectroscopy
  • Enzyme kinetics
  • Substrate evolution
  • Product evolution
  • Multiway


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