Abstract
A high-performance liquid chromatographic method for the simultaneous determination of both the stereo-chemical outcome and the cleavage pattern of enzymatic action on unmodified sugar substrates is described. Three different enzymes were investigated by this method. Human pancreatic α-amylase hydrolyzed maltopentaose with retention of anomeric configuration, with the cleavage position being two glucose units from the reducing end. Cellulomonas fimi endoglucanase D hydrolyzed cellopentaose with retention of anomeric configuration and predominantly two glucose units from the reducing end. β-D-Xylosidase from Butyrivibrio fibrisolvens hydrolyzed o-nitrophenyl β-D-xylopyranoside with inversion of anomeric configuration.
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