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
Format:	Artikel
Sprache:	eng
Schlagworte:	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
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Beschreibung
Zusammenfassung:	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.
ISSN:	1024-2422 1029-2446
DOI:	10.3109/10242420009015248