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Titolo:
Hydrolysis of sucrose by invertase immobilized onto novel magnetic polyvinylalcohol microspheres
Autore:
Akgol, S; Kacar, Y; Denizli, A; Arica, MY;
Indirizzi:
Hacettepe Univ, Dept Chem, TR-06532 Ankara, Turkey Hacettepe Univ AnkaraTurkey TR-06532 Dept Chem, TR-06532 Ankara, Turkey Kirikkale Univ, Dept Biol, TR-71450 Yahsihan, Kirikkale, Turkey Kirikkale Univ Yahsihan Kirikkale Turkey TR-71450 ihan, Kirikkale, Turkey
Titolo Testata:
FOOD CHEMISTRY
fascicolo: 3, volume: 74, anno: 2001,
pagine: 281 - 288
SICI:
0308-8146(200108)74:3<281:HOSBII>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
MEMBRANE; GLUCOAMYLASE; REACTOR; UREASE;
Keywords:
polyvinylalcohol; magnetite; microspheres; covalent bonding; enzyme immobilization; invertase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Arica, MY Hacettepe Univ, Dept Chem, TR-06532 Ankara, Turkey Hacettepe Univ Ankara Turkey TR-06532 TR-06532 Ankara, Turkey
Citazione:
S. Akgol et al., "Hydrolysis of sucrose by invertase immobilized onto novel magnetic polyvinylalcohol microspheres", FOOD CHEM, 74(3), 2001, pp. 281-288

Abstract

The magnetic polyvinylalcohol (PVAL) microspheres were prepared by crosslinking glutaraldehyde. 1,1 ' -Carbonyldiimidazole (CDI), a carbonylating agent was used for the activation of hydroxyl groups of polyvinylalcohol, and invertase immobilized onto the magnetic PVAL microspheres by covalent bonding through the amino group. The retained activity of the immobilized invertase was 74%. Kinetic parameters were determined for immobilized invertase, as well as for the free enzyme. The K-m values for immobilized invertase (55 mM sucrose) were higher than that of the free enzyme (24 mM sucrose), whereas V-max values were smaller for the immobilized invertase. The optimum operational temperature was 5 degreesC higher for immobilized enzyme than that of the free enzyme. The operational inactivation rate constant (k(opi)) of the immobilized invertase at 35 degreesC with 200 mM sucrose was 5.83 x 10(-5) min(-1). Thermal and storage stabilities were found to increase withimmobilization. (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 06/07/20 alle ore 08:21:44