title: Enzyme activity measurement via spectral evolution profiling and PARAFAC.
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.
authors: Center for BioProcess Engineering, Department of Chemical and Biochemical Engineering, Technical University of Denmark, Lyngby, Denmark.
authors: Andreas
authors: A
authors: Baum
authors: Anne S
authors: AS
authors: Meyer
authors: Javier Lopez
authors: JL
authors: Garcia
authors: Max
authors: M
authors: Egebo
authors: Per Waaben
authors: PW
authors: Hansen
authors: Jørn Dalgaard
authors: JD
authors: Mikkelsen
mesh_terms: D002138:Calibration / Q000592:standards; D002384:Catalysis; D002480:Cellulase / Q000737:chemistry / Q000378:metabolism*; D003124:Colorimetry; D057075:Enzyme Assays / Q000379:methods*; D005949:Glucose Oxidase / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D011133:Polysaccharide-Lyases / Q000737:chemistry / Q000378:metabolism*; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D005949:Glucose Oxidase; D002480:Cellulase; D011133:Polysaccharide-Lyases; C027349:pectin lyase