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Enzyme activity measurement via spectral evolution profiling and PARAFAC
Authors:Andreas Baum  Anne S Meyer  Javier Lopez Garcia  Max Egebo  Per Waaben Hansen  Jørn Dalgaard Mikkelsen
Institution:1. Center for BioProcess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark, DK-2800 Lyngby, Denmark;2. Foss Analytical, Foss Allé 1, DK-3400 Hillerød, Denmark
Abstract: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.
Keywords:Chemometrics  Fourier transform infrared spectroscopy  Enzyme kinetics  Substrate evolution  Product evolution  Multiway
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