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Titolo:
Stabilization of enzymes (D-amino acid oxidase) against hydrogen peroxide via immobilization and post-immobilization techniques
Autore:
Fernandez-Lafuente, R; Rodriguez, V; Mateo, C; Fernandez-Lorente, G; Arminsen, P; Sabuquillo, P; Guisan, JM;
Indirizzi:
CSIC, Dept Biocatalisis, Inst Catalisis, Lab Tecnol Enzimat, E-28049 Madrid, Spain CSIC Madrid Spain E-28049 sis, Lab Tecnol Enzimat, E-28049 Madrid, Spain
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 1-4, volume: 7, anno: 1999,
pagine: 173 - 179
SICI:
1381-1177(19990915)7:1-4<173:SOE(AO>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALDEHYDE-AGAROSE GELS; CEPHALOSPORIN-C; COVALENT ATTACHMENT; ACTIVATED SUPPORTS; TRANSFORMATION; DERIVATIVES; REDUCTION;
Keywords:
hydrogen peroxide; D-amino acid oxidase; enzyme stabilization; enzyme immobilization; chemical modification of enzymes; dextrans in chemistry of proteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Guisan, JM CSIC, Dept Biocatalisis, Inst Catalisis, Lab Tecnol Enzimat, Campus Univ Autonoma, E-28049 Madrid, Spain CSIC Campus Univ Autonoma MadridSpain E-28049 9 Madrid, Spain
Citazione:
R. Fernandez-Lafuente et al., "Stabilization of enzymes (D-amino acid oxidase) against hydrogen peroxide via immobilization and post-immobilization techniques", J MOL CAT B, 7(1-4), 1999, pp. 173-179

Abstract

Three different approaches are proposed to increase the resistance of enzymes against hydrogen peroxide. (a) Multipoint covalent immobilization. Through this technique, enzyme rigidity would be greatly increased and hence, any conformational change on the enzyme structure involved before or after oxidation with hydrogen peroxide becomes greatly prevented. (b) Oriented immobilization on supports having large internal surfaces. The immobilization of enzymes, through different areas of their surface on solid supports withinternal morphology composed by large surfaces, promotes a certain maskingof the enzyme areas that are very close to the support surface. In this way, the accessibility of hydrogen peroxide to such protein areas becomes greatly restricted. (c) Additional chemical modification of immobilized enzymederivatives with polymers. By adding thick barriers surrounding the whole enzyme molecule, the effective concentration of hydrogen peroxide in the proximity of the most sensitive residues may be strongly reduced. Multipoint covalently immobilized D-amino acid oxidase (DAAO) from Rhodotorula gracilis on glyoxyl-agarose is Ii-fold more stable than native enzyme against the deleterious effect of hydrogen peroxide. On the other hand, DAAO from Trigonopsis variabilis was not stabilized by rigidification but it could be highly stabilized by an adequate combination of the best orientation on the support plus an additional modification with poly-aldehyde polymers. (C) 1999 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 14:59:44