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Titolo:
UNUSUAL PROPERTIES OF THERMALLY SENSITIVE OLIGOMER-ENZYME CONJUGATES OF POLY(N-ISOPROPYLACRYLAMIDE)-TRYPSIN
Autore:
DING ZL; CHEN GH; HOFFMAN AS;
Indirizzi:
UNIV WASHINGTON,CTR BIOENGN,BOX 352255 SEATTLE WA 98195 UNIV WASHINGTON,CTR BIOENGN SEATTLE WA 98195
Titolo Testata:
Journal of biomedical materials research
fascicolo: 3, volume: 39, anno: 1998,
pagine: 498 - 505
SICI:
0021-9304(1998)39:3<498:UPOTSO>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYETHYLENE-GLYCOL; SOLUBLE POLYSACCHARIDES; TRYPSIN KINETICS; IMMOBILIZATION; CHYMOTRYPSIN; CELLULASE; STABILIZATION; BIOMOLECULES; DERIVATIVES; CATALYSIS;
Keywords:
PHASE-SEPARATED POLYMER; POLYMER-CONJUGATED PROTEINS; POLY(NIPAAM); TRYPSIN; ENZYME ACTIVITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
Z.L. Ding et al., "UNUSUAL PROPERTIES OF THERMALLY SENSITIVE OLIGOMER-ENZYME CONJUGATES OF POLY(N-ISOPROPYLACRYLAMIDE)-TRYPSIN", Journal of biomedical materials research, 39(3), 1998, pp. 498-505

Abstract

Reversible soluble-insoluble oligomer-enzyme conjugates have been prepared by conjugating a thermally sensitive oligomer, poly(N-isopropylacrylamide) [poly-(NIPAAm)] to trypsin. The conjugates can catalyze enzymatic reactions in solution and then may be separated from the solution by thermal precipitation. One special feature of the conjugates is that every poly(NIPAAm) chain has only one end attachment to the enzyme, so that the loss of enzymatic activity due to steric hindrance should be minimized. Conjugates with various numbers of oligomer chains per trypsin molecule were prepared. Surprisingly, the conjugates increased in enzymatic activity with increasing oligomer conjugation to the native trypsin. The trypsin active sites in the conjugates were accessible to large molecules, such as soybean trypsin inhibitor (MW = 21,500). The enzyme conjugates were more stable than native trypsin, both insolution and in the precipitated phase. On the other hand, the conjugates lost enzymatic activity faster than native trypsin when the temperature was repeatedly cycled through the lower critical solution temperature (LCST) of the poly(NIPAAm). The recovery of the conjugates by thermal precipitation in each cycle was over 95% even after 14 cycles through the LCST. (C) 1998 John Wiley & Sons, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 19:49:23