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Cellulase immobilized on copolymers based on N-vinylformamide: Influence of immobilization on the catalytic activity of the enzyme
Języki publikacji
Abstrakty
Badano wpływ immobilizacji celulazy z Aspergillus sp EC 3.2.1.4. na aktywność katalityczną w reakcji enzymatycznej hydrolizy celulozy. Celulazę immobilizowano na hydrofilowych polimerowych nośnikach z grupami formamidowymi i pierwszorzędowymi grupami aminowymi. Nośniki syntezowano w procesie wolnorodnikowej kopolimeryzacji strąceniowej N-winyloformamidu (NVF) z diwinylobenzenem (DVB). Reaktywne pierwszorzędowe grupy aminowe w kopolimerze generowano na drodze reakcji hydrolizy w środowisku alkalicznym. Celulazę immobilizowano kowalencyjnie za pośrednictwem aldehydu glutarowego (GA) na nośniku z grupami aminowymi lub adsorbowano na nośniku z grupami formamidowymi. Otrzymane heterogeniczne biokatalizatory testowano w reakcji hydrolizy celulozy mikrokrystalicznej. Stwierdzono, że aktywność celulazy immobilizowanej na obu badanych nośnikach była większa niż dla enzymu w stanie natywnym.
Immobilization effect of cellulase from Aspergillus sp. EC 3.2.1.4. catalytic activity in reaction of enzymatic hydrolysis of cellulose has been studied. Cellulase immobilized on a hydrophilic polymer carriers with formamide groups and primary amino groups. The carriers were synthesized in a free radical copolymerization of N-vinylformamide (NVF) with divinylbenzene (DVB). The reactive primary amino groups in the copolymer were generated by decarboxylation formamide groups in an alkaline medium. Cellulase was covalently immobilized via glutaraldehyde (GA) on the support with amino groups and adsorbed on a support with formamide groups. The resulting heterogeneous biocatalysts tested in the hydrolysis reaction microcrystalline cellulose. It was found that immobilized cellulase activity on both carriers tested was greater than the enzyme in the native state.
Czasopismo
Rocznik
Tom
Strony
447--454
Opis fizyczny
Bibliogr. 38 poz., rys., tab.
Twórcy
autor
- Wydział Chemii, Uniwersytet Jagielloński, Kraków
autor
- Instytut Chemii i Fizyki, Uniwersytet Rolniczy, Kraków
autor
- Wydział Chemii, Uniwersytet Jagielloński, Kraków
Bibliografia
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Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-b1498072-af8b-4288-83d9-440d645ff3b9