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Titolo:
Enantioselective enzymatic hydrolysis of racemic glycidyl esters by using immobilized porcine pancreas lipase with improved catalytic properties
Autore:
Pregnolato, M; Terreni, M; de Fuentes, IE; Leon, ARA; Sabuquillo, P; Fernandez-Lafuente, R; Guisan, JM;
Indirizzi:
Univ Pavia, Pharmaceut Biocatalysis Labs, Dip Chim Farmaceut, I-27100 Pavia, Italy Univ Pavia Pavia Italy I-27100 Dip Chim Farmaceut, I-27100 Pavia, Italy Univ Complutense, Dept Quim Organ & Farmaceut, Madrid 28040, Spain Univ Complutense Madrid Spain 28040 gan & Farmaceut, Madrid 28040, Spain CSIC, Dept Biocatalisis, Lab Tecnol Enzimat, Madrid 28040, Spain CSIC Madrid Spain 28040 talisis, Lab Tecnol Enzimat, Madrid 28040, Spain
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 4-6, volume: 11, anno: 2001,
pagine: 757 - 763
SICI:
1381-1177(20010122)11:4-6<757:EEHORG>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Keywords:
lipases; immobilization; hydrophobic adsorption; glycidyl butyrate; enantioselective hydrolyses;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
13
Recensione:
Indirizzi per estratti:
Indirizzo: Pregnolato, M Univ Pavia, Pharmaceut Biocatalysis Labs, Dip Chim Farmaceut, Via Palestro3, I-27100 Pavia, Italy Univ Pavia Via Palestro 3 Pavia Italy I-27100 Pavia, Italy
Citazione:
M. Pregnolato et al., "Enantioselective enzymatic hydrolysis of racemic glycidyl esters by using immobilized porcine pancreas lipase with improved catalytic properties", J MOL CAT B, 11(4-6), 2001, pp. 757-763

Abstract

The crude porcine pancreas lipase (PPL) extract is a mixture of several proteins (mainly lipases and esterases). In order to develop enzymatic catalysts with good catalytic properties for hydrolytic enantioselective reactions in aqueous homogeneous medium, we studied the immobilization of the different enzymes contained in the crude PPL extracts by selective sequential adsorption on hydrophobic supports bearing octyl, octadecyl and phenyl groups. Some minor proteins were selectively adsorbed on octyl and octadecyl supports while the most abundant lipase was adsorbed on the support bearing phenyl groups. The enantioselectivity of the different lipase derivatives weretested considering the hydrolysis of esters of 1,2-epoxi-1-propanol (glycidol). The most abundant lipase contained in the commercial crude PPL extract resulted almost inactive while some lipases contained in low concentrations displayed high activities and enantioselectivities. The most interestingresults were obtained with a 28-kDa protein selectively adsorbed on octyl-agarose. With this enzyme derivative, the residual butyric ester of glycidol was recovered with 96% enantiomeric excess at 55% conversion. (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 29/03/20 alle ore 09:30:41