A Novel Activity of Immobilized Penicillin G Acylase: Removal of Benzyloxycarbonyl Amino Protecting Group

A novel activity of penicillin G acylase from E. coli is presented. This enzyme, immobilized onto agarose gels by multipoint covalent attachment, was used for removing the benzyloxycarbonyl (Z) amino protecting group from selected amino acids and oligopeptides in different reaction systems. Quantita...

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Veröffentlicht in:Biocatalysis and biotransformation 2000, Vol.18 (3), p.253-258
Hauptverfasser: Alvaro, Gregorio, Feliu, Josep A., Caminal, Gloria, López-santín, Josep, Clapés, Pere
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container_end_page 258
container_issue 3
container_start_page 253
container_title Biocatalysis and biotransformation
container_volume 18
creator Alvaro, Gregorio
Feliu, Josep A.
Caminal, Gloria
López-santín, Josep
Clapés, Pere
description A novel activity of penicillin G acylase from E. coli is presented. This enzyme, immobilized onto agarose gels by multipoint covalent attachment, was used for removing the benzyloxycarbonyl (Z) amino protecting group from selected amino acids and oligopeptides in different reaction systems. Quantitative deprotection yields were obtained for simple amino acids, while the efficiency with oligopeptides varied depending on the sequence.
doi_str_mv 10.3109/10242420009015248
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ispartof Biocatalysis and biotransformation, 2000, Vol.18 (3), p.253-258
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source Taylor & Francis Journals Complete
subjects Amino acids
Antibiotics
benzyloxycarbonyl amino protecting group
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Enzyme kinetics
Enzymes and enzyme reactions
Escherichia coli
Fundamental and applied biological sciences. Psychology
Hydrolysis
Methods. Procedures. Technologies
oligopeptides
Organic solvents
penicillin G acylase
Peptides and polypeptides
Polypeptides
Synthesis (chemical)
Urethane protecting groups
title A Novel Activity of Immobilized Penicillin G Acylase: Removal of Benzyloxycarbonyl Amino Protecting Group
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