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Efficient cascade synthesis of ampicillin from penicillin G potassium salt using wild and mutant penicillin G acylase from Alcaligenes faecalis.

Authors :
Deng S
Ma X
Su E
Wei D
Source :
Journal of biotechnology [J Biotechnol] 2016 Feb 10; Vol. 219, pp. 142-8. Date of Electronic Publication: 2015 Dec 28.
Publication Year :
2016

Abstract

To avoid isolation and purification of the intermediate 6-aminopenicillanic acid (6-APA), a two-enzyme two-step cascade synthesis of ampicillin from penicillin G was established. In purely aqueous medium, penicillin G hydrolysis and ampicillin synthesis were catalyzed by immobilized wild-type and mutagenized penicillin G acylases from Alcaligenes faecalis (Af PGA), respectively (Fig. 1). The βF24 G mutant Af PGA (the 24th Phenylalanine of the β-subunit was replaced by Glycine) was employed for its superior performance in enzymatic synthesis of ampicillin. By optimizing the reaction conditions, including enzyme loading, temperature, initial pH and D-PGME/6-APA ratio, the conversion of the second step of ampicillin synthesis reached approximately 90% in 240 min and less than 1.7 mole D-PGME were required to produce 1 mole ampicillin. Overall, in a 285 min continuous two-step procedure, an ampicillin yield of 87% was achieved, demonstrating the possibility of improving the cascade synthesis of ampicillin by mutagenized PGA, providing an economically efficient and environmentally benign procedure for semi-synthetic penicillins antibiotics synthesis.<br /> (Copyright © 2015 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1873-4863
Volume :
219
Database :
MEDLINE
Journal :
Journal of biotechnology
Publication Type :
Academic Journal
Accession number :
26732414
Full Text :
https://doi.org/10.1016/j.jbiotec.2015.12.034