Original scientific paper

Quantitative Acylation of Amino Compounds Catalysed by Penicillin G Acylase in Organic Solvent at Controlled Water Activity

Alessandra Basso ; Dipartimento di Scienze Farmaceutiche, Universita degli Studi di Trieste, Piazzale Europa 1, 34127 Trieste, Italy
Stefania Biffi ; Dipartimento di Scienze Farmaceutiche, Universita degli Studi di Trieste, Piazzale Europa 1, 34127 Trieste, Italy
Luigi De Martin ; Dipartimento di Scienze Farmaceutiche, Universita degli Studi di Trieste, Piazzale Europa 1, 34127 Trieste, Italy
Lucia Gardossi ; Dipartimento di Scienze Farmaceutiche, Universita degli Studi di Trieste, Piazzale Europa 1, 34127 Trieste, Italy
Paolo Linda ; Dipartimento di Scienze Farmaceutiche, Universita degli Studi di Trieste, Piazzale Europa 1, 34127 Trieste, Italy

Abstract

Covalently immobilised penicillin G acylase (PGA-450) accepts in toluene, at controlled water activity (a_w), a broad range of amino compounds as nucleophiles in kinetically controlled acylation. Hydrolytic reactions were prevented and complete conversions were achieved in short times even when working with an equimolar concentration of the substrates. The recovery of the products was facile, leading to high isolation yields. The obtained N-acylated derivatives of L-amino acids can be used in further reactions, since no purification steps are required in such conditions. This opens new perspectives to the application of PGA in selective protection of the amino function for peptide synthesis. Ali attempts to perform esterification and transesterification reactions with PGA in toluene, at the same a_w as used for the acylation of amino compounds, were unsuccesful.

Keywords

penicillin G acylase; kinetically controlled synthesis; organic solvent; acylation; water activity; derivatised L-amino acids

Hrčak ID:

131952

URI

https://hrcak.srce.hr/131952

Publication date:

1.11.2001.

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