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Titolo:
Stabilization of a tetrameric enzyme (alpha-amino acid ester hydrolase from Acetobacter turbidans) enables a very improved performance of ampicillin synthesis
Autore:
Fernandez-Lafuente, R; Hernandez-Justiz, O; Mateo, C; Terreni, M; Alonso, J; Garcia-Lopez, JL; Moreno, MA; Guisan, JM;
Indirizzi:
Univ Autonoma Madrid, CSIC, Inst Catalisis, Dept Biocatalisis, E-28049 Madrid, Spain Univ Autonoma Madrid Madrid Spain E-28049 talisis, E-28049 Madrid, Spain CSIC, Ctr Invest Biol, E-28006 Madrid, Spain CSIC Madrid Spain E-28006CSIC, Ctr Invest Biol, E-28006 Madrid, Spain Antibiot SA, Leon, Spain Antibiot SA Leon SpainAntibiot SA, Leon, Spain
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 4-6, volume: 11, anno: 2001,
pagine: 633 - 638
SICI:
1381-1177(20010122)11:4-6<633:SOATE(>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
PENICILLIN-G ACYLASE; ESCHERICHIA-COLI; IMMOBILIZATION; CEPHALEXIN; AMIDASE;
Keywords:
stabilization of multimeric enzymes; enzymatic synthesis of ampicillin; stereospecific synthesis; enzyme specificity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
13
Recensione:
Indirizzi per estratti:
Indirizzo: Guisan, JM Univ Autonoma Madrid, CSIC, Inst Catalisis, Dept Biocatalisis, Campus UnivAutonoma, E-28049 Madrid, Spain Univ Autonoma Madrid Campus UnivAutonoma Madrid Spain E-28049
Citazione:
R. Fernandez-Lafuente et al., "Stabilization of a tetrameric enzyme (alpha-amino acid ester hydrolase from Acetobacter turbidans) enables a very improved performance of ampicillin synthesis", J MOL CAT B, 11(4-6), 2001, pp. 633-638

Abstract

The stabilized derivative of the enzyme ol-amino acid ester hydrolase fromAcetobacter turbidans has been found to be very adequate as biocatalyst ofthe synthesis of the very relevant antibiotic ampicillin. This enzyme resulted uch more adequate than the Penicillin G Acylase (PGA) from Escherichiacoli (the most used enzyme). The stabilization of the enzyme was required because under optimal conditions (absence of phosphate and 40% of MeOH), no-stabilized derivatives or soluble enzyme from A. turbidans become very rapidly inactivated. Under these conditions, this new stabilized derivative exhibited a very high selectivity for the transferase activity compared to the esterase one? as well as a very low hydrolytic activity towards the antibiotic. Moreover, this new biocatalyst did not recognize L-phenylglycine as substrate in the synthetic process. By using the racemic mixture of D/L phenylglycine methyl ester, 85% of the D-ester could be transformed to ampicillin. In contrast, the enzyme from E, coli exhibited a high hydrolytic activity for the ampicillin yielding low synthetic yields. This enzyme also resulted much less enantioselective producing both isomers of the antibiotic. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/06/20 alle ore 12:39:04