A novel bifunctional xylanase/cellulase TcXyn10A from Thermoascus crustaceus JCM12803.
- Author:
Xiaoli LI
1
;
Tao TU
2
;
Bin YAO
2
;
Xiangming XIE
1
;
Huiying LUO
2
Author Information
- Publication Type:Journal Article
- Keywords: Thermoascus crustaceus JCM12803; bifunctional enzyme; cellulase; xylanase
- MeSH: Cellulase; Endo-1,4-beta Xylanases; Enzyme Stability; Hydrogen-Ion Concentration; Molecular Docking Simulation; Pichia; Substrate Specificity; Thermoascus
- From: Chinese Journal of Biotechnology 2018;34(12):1996-2006
- CountryChina
- Language:Chinese
- Abstract: Efficient utilization of cellulose and xylan is of importance in the bioethanol industry. In this study, a novel bifunctional xylanase/cellulase gene, Tcxyn10a, was cloned from Thermoascus crustaceus JCM12803, and the gene product was successfully overexpressed in Pichia pastoris GS115. The recombinant protein was then purified and characterized. The pH and temperature optima of TcXyn10A were determined to be 5.0 and 65-70 °C, respectively. The enzyme retained stable under acid to alkaline conditions (pH 3.0-11.0) or after 1-h treatment at 60 °C. The specific activities of TcXyn10A towards beechwood xylan, wheat arabinoxylan, sodium carboxymethyl cellulose and lichenan were (1 480±26) U/mg, (2 055±28) U/mg, (7.4±0.2) U/mg and (10.9±0.4) U/mg, respectively. Homologous modeling and molecular docking analyses indicated that the bifunctional TcXyn10A has a single catalytic domain, in which the substrate xylan and cellulose shared the same binding cleft. This study provides a valuable material for the study of structure and function relationship of bifunctional enzymes.
