Biotechnology Letters, Vol.27, No.17, 1311-1317, 2005
Increased conformational and thermal stability properties for phenylalanine dehydrogenase by chemical glycosidation with end-group activated dextran
A mono-aminated dextran derivative was attached to Bacillus badius phenylalanine dehydrogenase via a carbodiimide-catalyzed reaction. The optimum temperature for the conjugate was 10 degrees C higher than for native enzyme, and its thermostability was improved by 8 degrees C. The activation free energy of thermal inactivation at 45 degrees C was increased by 16.8 kJ/mol. The improved conformational stability of the modified enzyme was confirmed by fluorescence spectroscopy.