Production of 6-aminopenicillanic acid in aqueous two-phase systems by recombinant Escherichia coli with intracellular penicillin acylase.
Bioconversion of penicillin G in PEG 20000/dextran T 70 aqueous two-phase systems was achieved using the recombinant Escherichia coli A56 (ppA22) with an intracellular penicillin acylase as catalyst. The best conversion conditions were attained for: 7% (w/v) substrate (penicillin G), enzyme activity in bottom phase 52 U ml(-1), pH 7.8, temperature 37 degrees C, reaction time 40 min. Five repeated batches could be performed in these conditions. Conversions ratios between 0.9-0.99 mol of 6-aminopenicillanic acid (6-APA) per mol of penicillin G, were obtained and volumetric productivity was 3.6-4.6 micromol min(-1) ml(-1). In addition the product 6-APA could be directly crystallized from the top phase with a purity of 96%.
Cao
Xue-jun
XJ
State Key Laboratory of Bioreactor Engineering, Department of Biochemical Engineering, East China University of Science and Technology, Shanghai 200237, PR China.
Wu
Xing-yan
XY
Fonseca
Luis J P
LJ
Cabral
Joaquim M S
JM
Marcos
João Carlos
JC
D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010397:Penicillanic Acid / Q000031:analogs & derivatives* / Q000737:chemistry*; D010399:Penicillin Amidase / Q000235:genetics* / Q000378:metabolism; D010400:Penicillin G / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D013696:Temperature
D011994:Recombinant Proteins; D010397:Penicillanic Acid; D010399:Penicillin Amidase; D010400:Penicillin G; C004408:aminopenicillanic acid