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

被引：0
作者：
Reynaldo Villalonga
Shinjiro Tachibana
Yunel Pérez
Yasuhisa Asano
机构：
[1] University of Matanzas,Enzyme Technology Group, Center for Biotechnological Studies
[2] Toyama Prefectural University,Biotechnology Research Center
来源：
Biotechnology Letters | 2005年 / 27卷
关键词：
dextran; enzyme stability; glycosidation; phenylalanine dehydrogenase;
D O I：
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中图分类号：
学科分类号：
摘要：
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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页码：1311 / 1317
页数：6
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