Chinese Journal of Catalysis ›› 2009, Vol. 30 ›› Issue (4): 291-296.

• Articles • Previous Articles     Next Articles

Increasing Activity of Lipase from Bacillus subtilis by Directed Evolution

ZHAO Bo, TAO Jin, MA Jisheng, LIAN Hong, WANG Yan, CHANG Lin, GAO Renjun*, CAO Shugui*   

  1. Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130023, Jilin, China
  • Received:2009-04-25 Online:2009-04-25 Published:2013-01-21

Abstract: Catalytic activity of a Bacillus subtilis lipase was enhanced by directed evolution. The distance between catalytic residue Ser77 and the substrate made an important contribution to the enzyme activity. The mutant lipase had lower energy, and its thermostability and pH stability were simultaneously increased.

Key words: Bacillus subtilis, lipase, error prone polymerase chain reaction, directed evolution, molecular docking