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Titolo:
Modulation of lipase properties in macro-aqueous systems by controlled enzyme immobilization: enantioselective hydrolysis of a chiral ester by immobilized Pseudomonas lipase
Autore:
Fernandez-Lorente, G; Terreni, M; Mateo, C; Bastida, A; Fernandez-Lafuente, R; Dalmases, P; Huguet, J; Guisan, JM;
Indirizzi:
CSIC, Dept Biocatalisis, Inst Catalisis, Madrid 28049, Spain CSIC MadridSpain 28049 iocatalisis, Inst Catalisis, Madrid 28049, Spain Vita Invest SA, Barcelona, Spain Vita Invest SA Barcelona SpainVita Invest SA, Barcelona, Spain
Titolo Testata:
ENZYME AND MICROBIAL TECHNOLOGY
fascicolo: 4-5, volume: 28, anno: 2001,
pagine: 389 - 396
SICI:
0141-0229(20010308)28:4-5<389:MOLPIM>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
PENICILLIN-G ACYLASE; INTERFACIAL ACTIVATION; HYDROPHOBIC SUPPORTS; SELECTIVE ADSORPTION; STABILIZATION; RESOLUTION; PROTEINS; COMPLEX; ACID;
Keywords:
enzymatic resolution of racemic mixtures; enzyme immobilization; modulation of enzyme properties; lipase from Pseudomonas fluorescens; 2-hydroxy 4-phenyl butanoic acid ethyl ester; lipase interfacial adsorption;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Guisan, JM CSIC, Dept Biocatalisis, Inst Catalisis, Campus UAM Cantoblanco, Madrid 28049, Spain CSIC Campus UAM Cantoblanco Madrid Spain 28049 id 28049, Spain
Citazione:
G. Fernandez-Lorente et al., "Modulation of lipase properties in macro-aqueous systems by controlled enzyme immobilization: enantioselective hydrolysis of a chiral ester by immobilized Pseudomonas lipase", ENZYME MICR, 28(4-5), 2001, pp. 389-396

Abstract

Lipase from Pseudomonas fluorescens (PFL) has been immobilized by using different immobilization protocols. The catalytic behavior of the different PFL derivatives in the hydrolytic resolution of f'ully soluble (R,S) 2-hydroxy l-phenyl butanoic acid ethyl ester (HPBE) in aqueous medium was analyzed. The soluble enzyme showed a significant but low enantioselectivity, hydrolyzing the S isomer more rapidly than the R-isomer (E = 7). The enzyme, immobilized via a limited attachment to a long and flexible spacer arm, showedalmost identical activity and specificity to the soluble enzyme. However, other derivatives, e.g. PFL adsorbed on supports covered by hydrophobic moieties (octyl, decaoctyl), exhibited significant hyperactivation on immobilization (approximately 7-fold). Simultaneously, the enantioselectivity of the PFL-immobilized enzyme was significantly improved (from E = 7 to E = 80). By using such derivatives, almost pure R eater isomer (e.e. > 99%) has been obtained after 55% hydrolysis of the racemic mixture of a solution of 10%(w/v) (R,S) HPBE. The derivatives could be used for 10 cycles without any significant decrease in the activity of the biocatalyst. (C) 2001 Elsevier Science Inc. All rights reserved.

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Documento generato il 07/07/20 alle ore 15:43:09