Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Activity of different Candida antarctica lipase B formulations in organic solvents
Autore:
Secundo, F; Carrea, G; Soregaroli, C; Varinelli, D; Morrone, R;
Indirizzi:
Ist Biocatalisi & Riconoscimento Mol, I-20131 Milan, Italy Ist Biocatalisi& Riconoscimento Mol Milan Italy I-20131 31 Milan, Italy ISSNIACF, CNR, Valverde, Italy ISSNIACF Valverde ItalyISSNIACF, CNR, Valverde, Italy
Titolo Testata:
BIOTECHNOLOGY AND BIOENGINEERING
fascicolo: 2, volume: 73, anno: 2001,
pagine: 157 - 163
SICI:
0006-3592(20010420)73:2<157:AODCAL>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PSEUDOMONAS-CEPACIA LIPASE; NONAQUEOUS MEDIA; ENZYME-ACTIVITY; WATER ACTIVITY; IMMOBILIZATION; PURIFICATION; ACTIVATION; STABILITY; CATALYSIS;
Keywords:
Candida antarctica lipase B; organic solvents; poly(ethylene-glycol); tramsesterification;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Secundo, F Ist Biocatalisi & Riconoscimento Mol, Via Mario Bianco 9, I-20131 Milan, Italy Ist Biocatalisi & Riconoscimento Mol Via Mario Bianco 9 Milan Italy I-20131
Citazione:
F. Secundo et al., "Activity of different Candida antarctica lipase B formulations in organic solvents", BIOTECH BIO, 73(2), 2001, pp. 157-163

Abstract

The activity of different formulations of Candida antarctica lipase B (CALB), such as crude CALB, purified CALB, purified CALB lyophilized with PEG (CALB + PEG) or oleic acid (CALB + GA), and the commercial formulation Novozym 435, was determined in toluene, carbon tetrachloride, and 1,4-dioxane atvarious water activities (a(w)). The reaction between vinylacetate and l-octanol was used as the model reaction and both transesterification (formation of 1-octylacetate) and hydrolytic (formation of acetic acid from vinylacetate) activities were determined. For equal amounts of lipase protein, CALB + PEG land to a lesser extent CALB + OA) displayed higher activity than that of the other formulations; for instance, in toluene (a(w) < 0.1), it was 260-, 13-, and 1.8-fold more active than crude CALB, purified CALB, and Novozym 435, respectively. Moreover, the transesterification activity of CALB + PEG was of the same order of magnitude (51%) of the activity shown by the enzyme in the hydrolysis of vinylacetate in aqueous buffer. These results suggest that PEG and oleic acid could act as lyoprotectants, preventing the formation of intermolecular interactions during the lyophilization process that might be responsible for protein denaturation. No diffusional limitation was observed for CALB + PEG-catalyzed reactions. Purified CALB, in contrast to the other formulations, showed a marked activity increase (2.1 to7.8-fold) as a function of a(w) and, in 1,4-dioxane, it was 3.5-fold more active when it was added to the solvent after previous dissolution of the lyophilized powder in water. <(c)> 2001 John Wiley & Sons, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 22:09:25