Baum, Andreas3; Meyer, Anne S.1; Garcia, Javier Lopez4; Egebo, Max5; Hansen, Per Waaben5; Mikkelsen, Jørn Dalgaard1
1 Department of Chemical and Biochemical Engineering, Technical University of Denmark2 Center for BioProcess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark3 Department of Applied Mathematics and Computer Science, Technical University of Denmark4 Technical University of Denmark5 FOSS Analytical A/S
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.