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Titolo:
Fourier-transform infrared spectroscopy study of dehydrated lipases from Candida antarctica B and Pseudomonas cepacia
Autore:
Vecchio, G; Zambianchi, F; Zacchetti, P; Secundo, F; Carrea, G;
Indirizzi:
CNR, Ist Biocatalisi & Riconoscimento Mol, I-20133 Milan, Italy CNR Milan Italy I-20133 alisi & Riconoscimento Mol, I-20133 Milan, Italy
Titolo Testata:
BIOTECHNOLOGY AND BIOENGINEERING
fascicolo: 5, volume: 64, anno: 1999,
pagine: 545 - 551
SICI:
0006-3592(19990905)64:5<545:FISSOD>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
SECONDARY STRUCTURE; ORGANIC-SOLVENTS; CRYSTAL-STRUCTURE; PROTEINS; CONFORMATION; SPECTRA; ALBUMIN; DENATURATION; ADSORPTION; INHIBITION;
Keywords:
Candida antarctica B lipase; Pseudomonas cepacia lipase; lyophilization; secondary structure; Fourier-transform infrared (FI-IR) spectroscopy;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Vecchio, G CNR, Ist Biocatalisi & Riconoscimento Mol, Via Mario Bianco 9, I-20133 Milan, Italy CNR Via Mario Bianco 9 Milan Italy I-20133 -20133 Milan, Italy
Citazione:
G. Vecchio et al., "Fourier-transform infrared spectroscopy study of dehydrated lipases from Candida antarctica B and Pseudomonas cepacia", BIOTECH BIO, 64(5), 1999, pp. 545-551

Abstract

Fourier-transform infrared (FT-IR) spectroscopy was employed to investigate potential lyophilization-induced changes in the secondary structure of lipases from Candida antarctica B and Pseudomonas cepacia. The secondary structure elements were determined by curve fitting of the amide III bands of the two lipases in the lyophilized state in KBr pellets and in solution. It was found that lyophilization decreased the alpha-helix and increased the beta-sheet content. However, FT-IR analysis of crosslinked enzyme crystals of Pseudomonas cepacia lipase also indicated an increase in the beta-sheet content, which appears despite the fact that the enzyme, being in the crystallized state, should possess native conformation. This result partially questions the suitability of FT-IR for analysis of the structure of solid proteins, at least as far as the beta-sheet content is concerned, because it ispossible that the method overestimates the beta-sheets by measuring other hydrogen-bonded nonperiodic intermolecular structures. No significant modification was observed when lipase from Pseudomonas cepacia was lyophilized in the presence of methoxypoly(ethylene glycol). (C) 1999 John Wiley & Sons,Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 00:59:34