Secreted expression of Bacillus pumilus xylanase gene in Pichia pastoris and study on enzymatic properties.
- Author:
Zheng-Bing JIANG
1
;
Hui-Ting SONG
;
Li-Xin MA
Author Information
1. College of Life science, Hubei University, Wuhan 430062, China.
- Publication Type:Journal Article
- MeSH:
Bacillus;
enzymology;
genetics;
Electrophoresis, Polyacrylamide Gel;
Endo-1,4-beta Xylanases;
genetics;
metabolism;
Hydrogen-Ion Concentration;
Pichia;
genetics;
metabolism;
Temperature
- From:
Chinese Journal of Biotechnology
2003;19(1):50-55
- CountryChina
- Language:Chinese
-
Abstract:
The endo-1,4-xylanase gene from Bacillus pumilus HB030 was cloned into the Pichia pastoris expression vector, pPIC9k, the recombinant plasmid was named pHBM220. The digested recombinant plasmid pHBM220 was transformed into Pichia pastoris KM71, GS115, SMD1168, respectively. The recombinant Pichia pastoris KM71 (pHBM220), GS115 (pHBM220), SMD1168 (pHBM220) secreted functional endo-1,4-xylanase, and the enzymatic activities reached 10.80IU/mL, 11.63IU/mL, 9.68IU/mL, respectively. The temperature and pH optimum for the recombinant xylanase were 60 degrees C and pH5.5, respectively.
