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Titolo:
A FUSION PROTEIN DESIGNED FOR NONCOVALENT IMMOBILIZATION - STABILITY,ENZYMATIC-ACTIVITY, AND USE IN AN ENZYME REACTOR
Autore:
STEMPFER G; HOLLNEUGEBAUER B; KOPETZKI E; RUDOLPH R;
Indirizzi:
UNIV HALLE WITTENBERG,INST BIOTECHNOL,KURT MOTHER STR 3 D-06120 HALLEGERMANY UNIV HALLE WITTENBERG,INST BIOTECHNOL D-06120 HALLE GERMANY BOEHRINGER MANNHEIM THERAPEUT D-82377 PENZBERG GERMANY
Titolo Testata:
Nature biotechnology
fascicolo: 4, volume: 14, anno: 1996,
pagine: 481 - 484
SICI:
1087-0156(1996)14:4<481:AFPDFN>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST ALPHA-GLUCOSIDASE; STABILIZATION; PURIFICATION; RESOLUTION;
Keywords:
FUSION PROTEIN; ENZYME IMMOBILIZATION; ENZYME REACTOR; PROTEIN STABILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
G. Stempfer et al., "A FUSION PROTEIN DESIGNED FOR NONCOVALENT IMMOBILIZATION - STABILITY,ENZYMATIC-ACTIVITY, AND USE IN AN ENZYME REACTOR", Nature biotechnology, 14(4), 1996, pp. 481-484

Abstract

We have designed a new method for enzyme immobilization using a fusion protein of yeast cli-glucosidase containing at its C-terminus a polycationic hexa-arginine fusion peptide. This fusion protein can be directly adsorbed from crude cell extracts on polyanionic matrices in a specific, oriented fashion. Upon noncovalent immobilization by polyionicinteractions, the stability of the fusion protein is not affected by pH-, urea-, or thermal-denaturation. Furthermore, the enzymatic properties (specific activity at increasing enzyme concentration, Michaelis constant, or activation energy of the enzymatic reaction) are not influenced by this noncovalent coupling. The operational stability of the coupled enzyme under conditions of continuous substrate conversion is,however, increased significantly compared to the soluble form. Fusionproteins containing polyionic peptide sequences are proposed as versatile tools for the production of immobilized enzyme catalysts.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 04:44:15