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.
Villalonga
Reynaldo
R
Enzyme Technology Group, Center for Biotechnological Studies, University of Matanzas, 44740, Matanzas, C.P, Cuba. reynaldo.villalonga@umcc.cu
Tachibana
Shinjiro
S
Pérez
Yunel
Y
Asano
Yasuhisa
Y
D000594:Amino Acid Oxidoreductases / Q000737:chemistry*; D001407:Bacillus / Q000201:enzymology*; D003911:Dextrans / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D006358:Hot Temperature; D011489:Protein Denaturation
D003911:Dextrans; D000594:Amino Acid Oxidoreductases; C022342:phenylalanine oxidase