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Titolo:
IONIC ADSORPTION OF CATALASE ON BIOSKIN - KINETIC AND ULTRASTRUCTURALSTUDIES
Autore:
SOLAS MT; VICENTE C; XAVIER L; LEGAZ ME;
Indirizzi:
UNIV COMPLUTENSE MADRID,FAC BIOL,DEPT PLANT PHYSIOL E-28040 MADRID SPAIN UNIV COMPLUTENSE MADRID,FAC BIOL,DEPT PLANT PHYSIOL E-28040 MADRID SPAIN UNIV COMPLUTENSE MADRID,FAC BIOL,DEPT CELL BIOL E-28040 MADRID SPAIN FED UNIV PARAIBA,CTR BIOTECHNOL RES,PHARMACEUT TECHNOL LAB BR-58000 JOAO PESSOA BRAZIL
Titolo Testata:
Journal of biotechnology
fascicolo: 1, volume: 33, anno: 1994,
pagine: 63 - 70
SICI:
0168-1656(1994)33:1<63:IAOCOB>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
HYDROLASE; XANTHAN;
Keywords:
BIOSKIN; CATALASE; IONIC ADSORPTION; IMMOBILIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
M.T. Solas et al., "IONIC ADSORPTION OF CATALASE ON BIOSKIN - KINETIC AND ULTRASTRUCTURALSTUDIES", Journal of biotechnology, 33(1), 1994, pp. 63-70

Abstract

Bioskin is a natural polymer produced by Acetobacter xylinum and several yeasts in culture. It contains glucosamine and N-acetyl galactosamine which promote ionic adsorption of catalase at the adequate pH value. High values of ionic strength are required to enzyme desorption. Adsorption of catalase on bioskin fibers has been visualized by scanningelectron microscopy associated to a dispersion X-ray analyzer. At lowenzyme density, the affinity of the immobilized catalase for hydrogenperoxide was 30% lower than that of the free enzyme. This affinity decreased dramatically at higher density of immobilized enzyme and couldnot be increased by agitation of the enzyme reaction mixture. Immobilized catalase retains about 70% of its initial activity after 16 d storage, whereas soluble enzyme is completely inactivated after 3 d at room temperature. The haeme group of catalase is not protected after immobilization since it is accessible to both EDTA and phloroglucinol, chelating agents which inactivate catalase by removing the iron atom from the haeme group.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 06:53:42