IMMOBILIZATION OF ENZYMES ON POLY(N-ACRYL OYLPIPERIDIN-4-ONE) - CHEMICAL INFLUENCE OF THE SUPPORT

Citation
J. Taillades et al., IMMOBILIZATION OF ENZYMES ON POLY(N-ACRYL OYLPIPERIDIN-4-ONE) - CHEMICAL INFLUENCE OF THE SUPPORT, Bulletin de la Societe chimique de France, 132(10), 1995, pp. 1021-1028
Citations number
28
Categorie Soggetti
Chemistry Inorganic & Nuclear",Biology,Chemistry
ISSN journal
00378968
Volume
132
Issue
10
Year of publication
1995
Pages
1021 - 1028
Database
ISI
SICI code
0037-8968(1995)132:10<1021:IOEOPO>2.0.ZU;2-E
Abstract
Poly(N-acryloylpiperidin-4-one) resin is an immobilization support of enzymes as varied as urease (hydrolase), glucose oxidase (oxidoreducta se) or pronase (protease). These preparations of immobilized enzymes h ave a good storage stability, an acceptable catalytic activity and a g ood stability in continuous functioning. Moreover, the ketonic functio ns (piperidin-4-one) of the support play an important role in the stab ility of the immobilized enzyme (glucose oxidase) and even in the sele ctivity of the enzymatic catalyst (pronase). In this work, the chemica l action of the support during catalysis allows the prevention of gluc ose oxidase deactivation by hydrogen peroxide, since the hydrogen pero xide produced by glucose oxidation in the presence of oxygen is fixed on the ketonic sites by the formation of alpha-hydroxyhydroperoxide.