Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop.
J Biotechnol
; 129(4): 717-22, 2007 May 10.
Article
em En
| MEDLINE
| ID: mdl-17350704
ABSTRACT
Xylitol dehydrogenase from Pichia stipitis (PsXDH) is one of the key enzymes for the bio-ethanol fermentation system from xylose. Previously, we constructed the C4 mutant (S96C/S99C/Y102C) with enhanced thermostability by introduction of structural zinc. In this study, for further improvement of PsXDH thermostability, we constructed the appropriate structural zinc-binding loop by comparison with other polyol dehydrogenase family members. A high thermostability of PsXDH was obtained by subsequent site-directed mutagenesis of the structural zinc-binding loop. The best mutant in this study (C4/F98R/E101F) showed a 10.8 degrees C higher thermal transition temperature (T(CD)) and 20.8 degrees C higher half denaturation temperature (T(1/2)) compared with wild-type.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pichia
/
D-Xilulose Redutase
Idioma:
En
Revista:
J Biotechnol
Assunto da revista:
BIOTECNOLOGIA
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Japão