Title of article :
Glycosidation of phenylalanine dehydrogenase with O-carboxymethyl-poly-β-cyclodextrin
Author/Authors :
Reynaldo Villalonga، نويسنده , , Shinjiro Tachibana، نويسنده , , Roberto Cao، نويسنده , , Madyu Matos، نويسنده , , Yasuhisa Asano، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2007
Pages :
5
From page :
471
To page :
475
Abstract :
The polysaccharide O-carboxymethyl poly-β-cyclodextrin (M = 1.3 × 104, 40% COOH groups) was employed as modification agent for Bacillus badius phenylalanine dehydrogenase via a carbodiimide-catalyzed reaction. The neoglycoenzyme retained 63% of its initial activity and contained about 2.5 mol of polymer per mole of enzyme. The optimum temperature for the enzyme was increased by 15 °C and its thermostability was improved by about 6 °C over 10 min incubation. The conjugate was also more resistant to thermal inactivation at different temperatures, ranging from 45 to 60 °C. The improved conformational stability of the modified enzyme was confirmed by fluorescence spectroscopy.
Keywords :
Phenylalanine dehydrogenase , Cyclodextrin , Enzyme stability , Glycosidation
Journal title :
Enzyme and Microbial Technology
Serial Year :
2007
Journal title :
Enzyme and Microbial Technology
Record number :
1174858
Link To Document :
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