Abstract
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 °C higher than for native enzyme, and its thermostability was improved by 8 °C. The activation free energy of thermal inactivation at 45 °C was increased by 16.8 kJ/mol. The improved conformational stability of the modified enzyme was confirmed by fluorescence spectroscopy.
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Villalonga, R., Tachibana, S., Pérez, Y. et al. Increased Conformational and Thermal Stability Properties for Phenylalanine Dehydrogenase by Chemical Glycosidation with End-group Activated Dextran. Biotechnol Lett 27, 1311–1317 (2005). https://doi.org/10.1007/s10529-005-3225-4
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DOI: https://doi.org/10.1007/s10529-005-3225-4