Highly efficient synthesis of ampicillin in an "aqueous solution-precipitate" system: Repetitive addition of substrates in a semicontinuous process

The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6‐aminopenicillanic acid (6‐APA). The yields of both 6‐APA and acyl donor could be improved by repetitively adding substrates to the reaction, a...

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Published in:Biotechnology and bioengineering Vol. 73; no. 5; pp. 426 - 430
Main Authors: Youshko, Maxim I., van Langen, Luuk M., de Vroom, Erik, van Rantwijk, Fred, Sheldon, Roger A., Švedas, Vytas K.
Format: Journal Article
Language:English
Published: New York John Wiley & Sons, Inc 05-06-2001
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Abstract The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6‐aminopenicillanic acid (6‐APA). The yields of both 6‐APA and acyl donor could be improved by repetitively adding substrates to the reaction, allowing the concentration of 6‐APA to remain saturated throughout. In this reaction concept, with four subsequent additions of substrates, 97% conversion of 6‐APA and 72% of D‐(−)‐phenylglycine methyl ester (D‐PGM) to ampicillin was achieved. The synthetic potential of this concept was estimated using a mathematical model which showed that by increasing the amount of added substrates a nearly quantitative conversion of 6‐APA and 85% conversion of acyl donor into ampicillin could be achieved . © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 426–430, 2001.
AbstractList The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6-aminopenicillanic acid (6-APA). The yields of both 6-APA and acyl donor could be improved by repetitively adding substrates to the reaction, allowing the concentration of 6-APA to remain saturated throughout. In this reaction concept, with four subsequent additions of substrates, 97% conversion of 6-APA and 72% of D-(-)-phenylglycine methyl ester (D-PGM) to ampicillin was achieved. The synthetic potential of this concept was estimated using a mathematical model which showed that by increasing the amount of added substrates a nearly quantitative conversion of 6-APA and 85% conversion of acyl donor into ampicillin could be achieved.
The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6‐aminopenicillanic acid (6‐APA). The yields of both 6‐APA and acyl donor could be improved by repetitively adding substrates to the reaction, allowing the concentration of 6‐APA to remain saturated throughout. In this reaction concept, with four subsequent additions of substrates, 97% conversion of 6‐APA and 72% of D‐(−)‐phenylglycine methyl ester (D‐PGM) to ampicillin was achieved. The synthetic potential of this concept was estimated using a mathematical model which showed that by increasing the amount of added substrates a nearly quantitative conversion of 6‐APA and 85% conversion of acyl donor into ampicillin could be achieved . © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 426–430, 2001.
The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus 6‐aminopenicillanic acid (6‐APA). The yields of both 6‐APA and acyl donor could be improved by repetitively adding substrates to the reaction, allowing the concentration of 6‐APA to remain saturated throughout. In this reaction concept, with four subsequent additions of substrates, 97% conversion of 6‐APA and 72% of D ‐(−)‐phenylglycine methyl ester (D‐PGM) to ampicillin was achieved. The synthetic potential of this concept was estimated using a mathematical model which showed that by increasing the amount of added substrates a nearly quantitative conversion of 6‐APA and 85% conversion of acyl donor into ampicillin could be achieved . © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 426–430, 2001.
Author Sheldon, Roger A.
van Langen, Luuk M.
Švedas, Vytas K.
de Vroom, Erik
van Rantwijk, Fred
Youshko, Maxim I.
Author_xml – sequence: 1
  givenname: Maxim I.
  surname: Youshko
  fullname: Youshko, Maxim I.
  organization: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119899 Moscow, Russia; fax: +7 095 9393181
– sequence: 2
  givenname: Luuk M.
  surname: van Langen
  fullname: van Langen, Luuk M.
  organization: Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Delft, The Netherlands
– sequence: 3
  givenname: Erik
  surname: de Vroom
  fullname: de Vroom, Erik
  organization: DSM Anti-Infectives, Delft, The Netherlands
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  givenname: Fred
  surname: van Rantwijk
  fullname: van Rantwijk, Fred
  organization: Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Delft, The Netherlands
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  givenname: Roger A.
  surname: Sheldon
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  organization: Laboratory of Organic Chemistry and Catalysis, Delft University of Technology, Delft, The Netherlands
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  givenname: Vytas K.
  surname: Švedas
  fullname: Švedas, Vytas K.
  email: Vytas@enzyme.genebee.msu.su
  organization: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119899 Moscow, Russia; fax: +7 095 9393181
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Snippet The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus...
The synthesis of ampicillin catalyzed by Escherichia coli penicillin acylase was optimized in an aqueous system with partially dissolved antibiotic nucleus...
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SubjectTerms 6-aminopenicillanic acid
ampicillin
Ampicillin - metabolism
ampicillin synthesis
aqueous biocatalytic process
aqueous solution-precipitate system
Chemical Precipitation
D-(-)-phenylglycine methyl ester
Escherichia coli
Escherichia coli - enzymology
Models, Theoretical
Penicillanic Acid - analogs & derivatives
Penicillanic Acid - metabolism
penicillin acylase
Penicillin Amidase - metabolism
Solutions
Water
Title Highly efficient synthesis of ampicillin in an "aqueous solution-precipitate" system: Repetitive addition of substrates in a semicontinuous process
URI https://api.istex.fr/ark:/67375/WNG-JZDJZ9P4-6/fulltext.pdf
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fbit.1076
https://www.ncbi.nlm.nih.gov/pubmed/11320513
https://search.proquest.com/docview/18150564
https://search.proquest.com/docview/70809200
Volume 73
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