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Rational design of a more stable penicillin G acylase against organic cosolvent
Authors:Sheng Yang   Liping Zhou   Haixu Tang   Jiang Pan   Xingjia Wu   He Huang  Zhongyi Yuan  
Affiliation:

Institute of Biochemistry and Cell Biology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China

Abstract:We have used a simple and efficient approach by combining the known functional and structural properties of penicillin G acylase (PGA) from E. coli, and tried to mutate PGA of Bacillus megaterium with the goal of increasing the stability of the enzyme in organic solvents or at acidic pH. The PGA mutants Kβ427A, Kβ430A and Kβ427A/Kβ430A obtained have higher stability in DMF than the wild-type PGA.
Keywords:Penicillin G acylase   Protein stability   Protein engineering
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