Improving the thermostability of Trichoderma reesei xylanase 2 by introducing disulfide bonds
Electron. j. biotechnol
;
26: 52-59, Mar. 2017. ilus, tab, graf
Artículo
en Inglés
| LILACS
| ID: biblio-1008980
ABSTRACT
Background: Xylanases are considered one of the most important enzymes in many industries. However, their low thermostability hampers their applications in feed pelleting, pulp bleaching, and so on. The main aim of this work was to improve the thermostability of Trichoderma ressei xylanase 2 (Xyn2) by introducing disulfide bonds between the N-terminal and α-helix and the ß-sheet core. Results: In this work, two disulfide bonds were separately introduced in the Xyn2 to connect the N-terminal and α-helix to the ß-sheet core of Xyn2. The two disulfide bonds were introduced by site-directed mutagenesis of the corresponding residues. The half-life of the mutants Xyn2C1452 (disulfide bond between ß-sheets B2 and B3) and Xyn2C59149 (disulfide bond between ß-sheets A5 and A6) at 60°C was improved by approximately 2.5- and 1.8-fold compared to that of the wild type Xyn2. In addition, the enzyme's resistance to alkali and acid was enhanced. Conclusion: Our results indicated that the connection of the N-terminal and α-helix to the ß-sheet core is due to the stable structure of the entire protein.
Texto completo:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
Trichoderma
/
Xilosidasas
/
Disulfuros
Idioma:
Inglés
Revista:
Electron. j. biotechnol
Asunto de la revista:
Biotecnologia
Año:
2017
Tipo del documento:
Artículo
/
Documento de proyecto
País de afiliación:
China
Institución/País de afiliación:
Sichuan Agricultural University/CN
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