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Titolo:
Biocatalyst engineering exerts a dramatic effect on selectivity of hydrolysis catalyzed by immobilized lipases in aqueous medium
Autore:
Fernandez-Lorente, G; Fernandez-Lafuente, R; Palomo, JM; Mateo, C; Bastida, A; Coca, J; Haramboure, T; Hernandez-Justiz, O; Terreni, M; Guisan, JM;
Indirizzi:
Univ Autonoma Madrid, CSIC, Inst Catalisis, Dept Biocatalysis, E-28049 Madrid, Spain Univ Autonoma Madrid Madrid Spain E-28049 talysis, E-28049 Madrid, Spain ISPJAE, Polytech Inst, Dept Chem Engn, Havana, Cuba ISPJAE Havana CubaISPJAE, Polytech Inst, Dept Chem Engn, Havana, Cuba Univ Pavia, Dept Pharmaceut Chem, I-27100 Pavia, Italy Univ Pavia Pavia Italy I-27100 ept Pharmaceut Chem, I-27100 Pavia, Italy
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 4-6, volume: 11, anno: 2001,
pagine: 649 - 656
SICI:
1381-1177(20010122)11:4-6<649:BEEADE>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
CANDIDA-RUGOSA LIPASES; HYDROPHOBIC SUPPORTS; ADSORPTION; RESOLUTION; ESTERS;
Keywords:
selective hydrolysis; immobilized lipases; modulation of selectivity of lipases; mandelic acid;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Guisan, JM Univ Autonoma Madrid, CSIC, Inst Catalisis, Dept Biocatalysis, Campus UnivAutonoma, E-28049 Madrid, Spain Univ Autonoma Madrid Campus UnivAutonoma Madrid Spain E-28049
Citazione:
G. Fernandez-Lorente et al., "Biocatalyst engineering exerts a dramatic effect on selectivity of hydrolysis catalyzed by immobilized lipases in aqueous medium", J MOL CAT B, 11(4-6), 2001, pp. 649-656

Abstract

It has been found that enantioselectivity of lipases is strongly modified when their immobilization is performed by involving different areas of the enzyme surface, by promoting a different degree of multipoint covalent immobilization or by creating different environments surrounding different enzyme areas. Moreover, selectivity of some immobilized enzyme molecules was much more modulated by the experimental conditions than other derivatives. Thus, some immobilized derivatives of Candida rugosa (CRL) and C. antarctica-B (CABL) Lipases are hardly enantioselective in the hydrolysis of chiral esters of (R,S)-mandelic acid under standard conditions (pH 7.0 and 25 degreesC) (E < 2). However, other derivatives of the same enzymes exhibited a very good enantioselectivity under nonstandard conditions. For example, CRL, adsorbed on PEI-coated supports showed a very high enantio-preference towards S-isomer (E = 200) at pH 5. On the other hand, CABL adsorbed on octyl-agarose showed an interesting enantio-preference towards the R-isomer (E = 25)at pH 5 and 4<degrees>C. These biotransformations are catalyzed by isolated lipase molecules acting on fully soluble substrates and in the absence ofinterfacial activation against external hydrophobic interfaces. Under these conditions, lipase catalysis may be associated to important conformational changes that can be strongly modulated via biocatalyst and biotransformation engineering. In this way, selective biotransformations catalyzed by immobilized lipases in macro-aqueous systems can be easily modulated by designing different immobilized derivatives and reaction conditions. (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 07/07/20 alle ore 22:19:55