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Updated: Aug 15, 2026

Genetic Incorporation of Biosynthesized L-dihydroxyphenylalanine (DOPA) and Its Application to Protein Conjugation
Published on: August 24, 2018
Increased conformational and thermal stability properties for phenylalanine dehydrogenase by chemical glycosidation
Reynaldo Villalonga1, Shinjiro Tachibana, Yunel Pérez
1Enzyme Technology Group, Center for Biotechnological Studies, University of Matanzas, 44740, Matanzas, C.P, Cuba. reynaldo.villalonga@umcc.cu
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 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.
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