Title of article :
Rational design of a more stable penicillin G acylase against organic cosolvent
Author/Authors :
Yang، نويسنده , , Sheng and Zhou، نويسنده , , Liping and Tang، نويسنده , , Haixu and Pan، نويسنده , , Jiang and Wu، نويسنده , , Xingjia and Huang، نويسنده , , He and Yuan، نويسنده , , Zhongyi، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2002
Pages :
6
From page :
285
To page :
290
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
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2002
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1709408
Link To Document :
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