Biotechnology Bulletin ›› 2013, Vol. 0 ›› Issue (2): 130-134.

• Research report • Previous Articles     Next Articles

Heterologous Expression and Characterization of Xylanase XYA6205 from Stachybotrys chartarum

Wang Hongxia1,2 Wang Huaming2 Zhang Dalong2 Luo Cheng1   

  1. (1. Key Laboratory of Food Nutrition and Safety, Tianjin University of Science and Technology, Ministry of Education, School of Food
  • Received:2012-09-03 Revised:2013-02-27 Online:2013-02-26 Published:2013-02-27
  • Contact: 王华明,男,博士,教授,博士生导师,研究方向:蛋白质表达,新型工业酶及表达系统;E-mail :wang_hm@tib.cas.cn

Abstract: Xylanase, the main enzyme to hydrolysis hemicellulose, has important application in industry. In this study, a gene xya6205 (with signal peptide)from Stachybotrys chartarum was inserted to an expression vector, eventually an recombinant plasmid pGm-xya6205 was constructed, and then transformed into A. niger G1 mediated by PEG4000. The transformants were confirmed by PCR analysis, and the recombinant xylanase of heterologously expressed protein in SDS-PAGE was about 20 kD. The optimal temperature and pH of the enzyme activity was 50℃ and 5.8, respectively. The recombinant enzyme specific activity reached 392 U/mg by DNS method at optimal condition. The recombinant enzyme remained 83% activity after 18 h in the alkaline buffer.

Key words: Xylanase, Aspergillus niger, Cloning, Activity, Stachybotrys chartarum