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Titolo:
PREPARATION AND PROPERTIES OF THERMOREVERSIBLE, PHASE-SEPARATING ENZYME-OLIGO(N-ISOPROPYLACRYLAMIDE) CONJUGATES
Autore:
CHEN GH; HOFFMAN AS;
Indirizzi:
UNIV WASHINGTON,CTR BIOENGN,FL-20 SEATTLE WA 98195 UNIV WASHINGTON,CTR BIOENGN,FL-20 SEATTLE WA 98195
Titolo Testata:
Bioconjugate chemistry
fascicolo: 6, volume: 4, anno: 1993,
pagine: 509 - 514
SICI:
1043-1802(1993)4:6<509:PAPOTP>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
SOLUBLE POLYSACCHARIDES; IMMOBILIZED ENZYMES; PROTEIN CONJUGATION; POLYMER; STABILIZATION; CHYMOTRYPSIN; DERIVATIVES; CELLULASE; CATALYSIS; STABILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
G.H. Chen e A.S. Hoffman, "PREPARATION AND PROPERTIES OF THERMOREVERSIBLE, PHASE-SEPARATING ENZYME-OLIGO(N-ISOPROPYLACRYLAMIDE) CONJUGATES", Bioconjugate chemistry, 4(6), 1993, pp. 509-514

Abstract

A thermoreversible N-isopropylacrylamide (NIPAAm) oligomer with an N-hydroxysuccinimide (NHS) ester functional end group has been prepared for coupling to an enzyme, beta-D-glucosidase, to form a thermoreversible, phase-separating polymer-enzyme conjugate. This conjugate can be used for separation, recovery, and recycle of an enzyme simply by applying small temperature changes to the reaction medium. In contrast to the random polymer-enzyme conjugates previously reported by us and others in the literature, in this study the conjugate is formed by a single, end attachment of each oligomer chain to the enzyme. Preliminary studies show that the conjugated enzyme exhibits very high retention ofactivity, even higher than native enzyme, and shows improved thermal stability compared to native enzyme.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 12:06:38