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Titolo:
Protein-containing hydrophobic coatings and films
Autore:
Novick, SJ; Dordick, JS;
Indirizzi:
Rensselaer Polytech Inst, Dept Chem Engn, Troy, NY 12180 USA Rensselaer Polytech Inst Troy NY USA 12180 Chem Engn, Troy, NY 12180 USA Univ Iowa, Dept Chem & Biochem Engn, Iowa City, IA 52242 USA Univ Iowa Iowa City IA USA 52242 & Biochem Engn, Iowa City, IA 52242 USA
Titolo Testata:
BIOMATERIALS
fascicolo: 2, volume: 23, anno: 2002,
pagine: 441 - 448
SICI:
0142-9612(200201)23:2<441:PHCAF>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALPHA-CHYMOTRYPSIN; ORGANIC-SOLVENTS; BIOSENSOR; MICELLES; ENZYMES; POLYMER; TRYPSIN;
Keywords:
enzyme polymer composites; biocatalytic coatings and films; antifouling materials;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
20
Recensione:
Indirizzi per estratti:
Indirizzo: Dordick, JS Rensselaer Polytech Inst, Dept Chem Engn, Troy, NY 12180 USA Rensselaer Polytech Inst Troy NY USA 12180 Troy, NY 12180 USA
Citazione:
S.J. Novick e J.S. Dordick, "Protein-containing hydrophobic coatings and films", BIOMATERIAL, 23(2), 2002, pp. 441-448

Abstract

The incorporation of enzymes and other proteins into hydrophobic polymericcoatings and films has been investigated in this study with the goal of generating biologically active materials for biocatalysis, antifouling surfaces, and biorecognition. The protein-polymer composites are created using standard solution coating techniques with poly(methyl methacrylate), polystyrene, and poly(vinyl acetate) as polymers and alpha -chymotrypsin and trypsin as biocatalysts. The specific enzyme is first extracted into a nonpolar organic solvent using hydrophobic ion-pairing. The ion-paired enzyme is dried and redissolved into a solvent also miscible with the polymer. This solution is then poured over a surface and the solvent is allowed to evaporate to form the enzyme-containing coating, which can then be delaminated to forma film. Leaching of enzyme from and activity of the biocatalytic coatings and films were evaluated. The biocatalytic coatings showed no loss of activity over ca. one week. For the biocatalytic films, the leaching rate was initially high followed by a slow rate of enzyme loss. Activity was measurable for at least one month, with only ca. one-third of the initial activity lost in that time, while, being continuously incubated in a buffer solution. Activity was also exhibited on macromolecular (protein) substrates. The biocatalytic coatings could be reused over 100 times with only a modest loss of activity. Finally, coatings and films containing a lectin (Concanavalin A) were capable of selectively binding to glycoproteins, thereby extending the application of such films for use in bioseparations and biorecognition. (C) 2001 Elsevier Science Ltd. 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 17:11:34