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Titolo:
Immobilized enzymes in ordered mesoporous silica materials and improvementof their stability and catalytic activity in an organic solvent
Autore:
Takahashi, H; Li, B; Sasaki, T; Miyazaki, C; Kajino, T; Inagaki, S;
Indirizzi:
Toyota Cent Res & Dev Labs Inc, Nagakute, Aichi 4801192, Japan Toyota CentRes & Dev Labs Inc Nagakute Aichi Japan 4801192 801192, Japan
Titolo Testata:
MICROPOROUS AND MESOPOROUS MATERIALS
, volume: 44, anno: 2001,
pagine: 755 - 762
SICI:
1387-1811(200106)44:<755:IEIOMS>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALKYLTRIMETHYLAMMONIUM-KANEMITE COMPLEXES; POLYETHYLENE-GLYCOL; CAPSULE MEMBRANES; MOLECULAR-SIEVE; COPOLYMER; TRIBLOCK; PERMEABILITY; CONVERSION; LIPASE;
Keywords:
enzyme immobilization; mesoporous materials; pore size; stabilization; surface characteristics;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Takahashi, H Toyota Cent Res & Dev Labs Inc, 41-1, Nagakute, Aichi 4801192, Japan Toyota Cent Res & Dev Labs Inc 41-1 Nagakute Aichi Japan 4801192
Citazione:
H. Takahashi et al., "Immobilized enzymes in ordered mesoporous silica materials and improvementof their stability and catalytic activity in an organic solvent", MICROP M M, 44, 2001, pp. 755-762

Abstract

Enzyme immobilization in mesoporous materials with various pore sizes was studied. The size of the mesopores was controlled by means of the combination of the alkyl chain lengths of surfactants and a swelling agent (triisopropyl benzene). Enzymes were selectively adsorbed to FSM-16 and MCM-41 prepared with a cationic surfactant. whose pore sizes were over the molecular diameters of the enzymes. and were not adsorbed significantly to SBA-15 prepared with a non-ionic surfactant. The higher adsorption as to FSM-16 or MCM-11 rather than on SBA-lj may be due to the ionic characteristics of the mesopore. which would be consistent with the observed larger adsorption capacity as to the cationic pigment rather than the anionic pigment of these materials. Enzymes, horseradish peroxidase and subtilisin, immobilized in FSM-16 showed the best stability and peak catalytic activity in an organic solvent when the average mesopore size just exceeded the molecular diameters of the enzymes. (C) 2001 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 03/06/20 alle ore 09:23:28