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Titolo:
Evaluation of different enzymes as catalysts for the production of beta-lactam antibiotics following a kinetically controlled strategy
Autore:
Hernandez-Justiz, O; Terreni, M; Pagani, G; Garcia, JL; Guisan, JM; Fernandez-Lafuente, R;
Indirizzi:
Univ Autonoma Madrid, CSIC, Inst Catalysis, Technol Enzymat Lab, E-28049 Madrid, Spain Univ Autonoma Madrid Madrid Spain E-28049 mat Lab, E-28049 Madrid, Spain Univ Pavia, Dipartimento Chim Farmaceut, I-27100 Pavia, Italy Univ Pavia Pavia Italy I-27100 ento Chim Farmaceut, I-27100 Pavia, Italy CSIC, Ctr Invest Biol, E-28006 Madrid, Spain CSIC Madrid Spain E-28006CSIC, Ctr Invest Biol, E-28006 Madrid, Spain
Titolo Testata:
ENZYME AND MICROBIAL TECHNOLOGY
fascicolo: 3-5, volume: 25, anno: 1999,
pagine: 336 - 343
SICI:
0141-0229(199908)25:3-5<336:EODEAC>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PENICILLIN-G ACYLASE; IMMOBILIZATION-STABILIZATION; KLUYVERA-CITROPHILA; ACTIVATED SUPPORTS; EQUILIBRIUM; YIELDS;
Keywords:
enzymatic synthesis of antibiotics; ampicillin; cephalexin; cephamandole; aqueous two-phase system;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Fernandez-Lafuente, R Univ Autonoma Madrid, CSIC, Inst Catalysis, Technol Enzymat Lab, E-28049 Madrid, Spain Univ Autonoma Madrid Madrid Spain E-28049 d, Spain
Citazione:
O. Hernandez-Justiz et al., "Evaluation of different enzymes as catalysts for the production of beta-lactam antibiotics following a kinetically controlled strategy", ENZYME MICR, 25(3-5), 1999, pp. 336-343

Abstract

Several beta-lactam acylases produced by different microorganisms (Escherichia coli, Kluyvera citrophila, Acetobacter turbidans, and Bacillus megaterium) have been evaluated as catalysts for the syntheses of relevant beta-lactam antibiotics (ampicillin, cephalexin, and cefamandole). These enzymes displayed very different synthetic properties showing large differences in synthetic yields (by a 4- to 5-fold factor) depending on the antibiotic and the enzyme. The enzyme from A. turbidans presented the best properties for the synthesis of ampicillin, which is a low activity in the hydrolysis of the antibiotic and a high specificity for the transformation of the ester into antibiotic. Although this enzyme was able to transform approximately 80%of phenylglycine methyl ester into ampicillin, it was unsuitable for the synthesis of cephalexin and cefamandole. In fact, all of the enzymes showed significant hydrolysis rates of the antibiotics compared to the synthetic activity, although the enzyme from E. coli exhibited the highest specificityfor the transformation of eaters into these antibiotics. To prevent the hydrolysis of the antibiotic, a two-phase aqueous system was used to extract the antibiotic from the enzyme environment. In this way, high synthetic yields could be obtained, e.g. 80% of phenylglycine methyl ester was transformed into cephalexin using the enzyme from E. coli. (C) 1999 Elsevier ScienceInc. All rights reserved.

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Documento generato il 16/07/20 alle ore 06:41:15