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Chinese Journal of Biotechnology ; (12): 623-629, 2010.
Artículo en Chino | WPRIM | ID: wpr-292228

RESUMEN

We engineered a disulphide bridge between two adjacent double-layered beta-sheet at the N-terminal region of Trichoderma reesei endo-1,4-beta-xylanase II(XYN II) by site-directed mutagenesis. The native xylanase XYN-OU and the mutated xylanase XYN-HA12 (T2C, T28C and S156F) were separately expressed in Pichia pastoris. Both xylanases were purified and characterized. The optimum temperature of XYN-HA12 was increased from 50 degrees C to 60 degrees C, relative to XYN-OU. At 70 degrees C, the halftime of inactivation for XYN-OU and XYN-HA12 were 1 min and 14 min, respectively. The optimum pH of XYN-HA12 was 5.0, similar to XYN-OU. However, XYN-HA12 could retain over 50% activity from pH 3.0 to 10.0 at 50 degrees C for 30 min. As for XYN-OU, it could retain over 50% activity from the pH value 4.0 to 9.0 at 50 degrees C in 30 min. The result of the mutated xylanase indicated that constructed disulphide bridge could improve its thermostability at relatively higher temperature.


Asunto(s)
Sustitución de Aminoácidos , Disulfuros , Química , Metabolismo , Endo-1,4-beta Xilanasas , Química , Genética , Estabilidad de Enzimas , Genética , Mutagénesis Sitio-Dirigida , Pichia , Genética , Metabolismo , Ingeniería de Proteínas , Métodos , Proteínas Recombinantes , Química , Trichoderma , Genética
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