Increased Conformational and Thermal Stability Properties for Phenylalanine Dehydrogenase by Chemical Glycosidation with End-group Activated Dextran

Authors: Villalonga, Reynaldo¹; Tachibana, Shinjiro²; Pérez, Yunel³; Asano, Yasuhisa²

Source: Biotechnology Letters, Volume 27, Number 17, September 2005 , pp. 1311-1317(7)

Publisher: Springer

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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.

Keywords: dextran; enzyme stability; glycosidation; phenylalanine dehydrogenase

Document Type: Research article

DOI: http://dx.doi.org/10.1007/s10529-005-3225-4

Affiliations: 1: Enzyme Technology Group, Center for Biotechnological Studies, University of Matanzas, 44740, Matanzas, C.P, Cuba, Email: reynaldo.villalonga@umcc.cu 2: Biotechnology Research Center, Toyama Prefectural University, 5180 Kurokawa, 939-0398, Kosugi, Toyama, Japan, 3: Enzyme Technology Group, Center for Biotechnological Studies, University of Matanzas, 44740, Matanzas, C.P, Cuba,

Publication date: 2005-09-01