Polymères Bioactifs X. Insolubilisation de la β‐Amylase sur des Dérivés de la Cellulose

Simionescu, Cr.; Bouzaher, Y.; Dumitriu, Severian

doi:10.1002/bscb.19810900909

Bulletin des Soc Chimique

1981

DOI: 10.1002/bscb.19810900909

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Polymères Bioactifs X. Insolubilisation de la β‐Amylase sur des Dérivés de la Cellulose

Cr. Simionescu¹,

Y. Bouzaher²,

Severian Dumitriu³

Abstract: Insolubilization of @-amylase on cellulose carbonate and aminoaromatic derivatives of carboxymethylcellulose (CMC), such as N-(rl-aminophenyl)-CMC amide and N-(4,4'-diaminodibenzyl)-CMC amide, is presented. The optimum coupling conditions depend on the nature of the carrier. By comparing the kinetic data for the reactions of insolubilized enzymes some conclusions are drawn regarding the influence of the support and of the binding mode on the activity of the coupled enzyme. INTRODUCTIONLes enzymes, biocatalysat… Show more

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Cited by 5 publications

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Bioactive polymers. XIII. Carrier nature and the insolubilization conditions of enzymes

Dumitriu¹,

Bulacovschi²,

Baston³

et al. 1984

Acta Polymerica

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Acta Polymerica 35 (19W) Nr. 8 536 DUMITRIU, BULACOVSCHI et al. : Bioactive polymers. XI11 Feinstruktur aufweist, und ist die Kerbwirkung stark genug, dann zerreifit das Filament unter Bildung der rauhen Restbruchflache schlagartig. In vielen Fallen wird die Restbruchflache von lappenformigen, iiberstehenden Fasermantelschichten umgeben. Das Bild 3 gibt rasterelektronenmikroskopische Aufnahmen je eines Filaments mit hoher, rnit mittlerer und mit niedriger Bruchspannung wieder. Aus den Bildern sind keine Erklarungen abzuleiten, warum die Kapillaren bei unterschiedlichen Spannungen durchreiaen. Bei den Faden rnit niedriger Bruchdehnung oder niedriger Bruchfestigkeit findet man in Ausnahmefallen, daB der Bruch auf zwei gegenuberliegenden Seiten eines Filaments gleichzeitig begonnen hat (Bild 4a), dafi kristallartige Ablagerungen a n der Oberflache vorliegen (Bilder 4b, 4c) oder daS eine abweichende Bruchmorphologie auftritt (4d). Auffallig ist, dafi die beiden Bruchenden eines Monofilaments in fast allen Fallen die gleiche Kerbenform aufweisen (Bild 3). Man konnte sich vorstellen, daI3 ein Bruch dort beginnt, wo zwei Fehlstellen dicht benachbart beieinander liegen. Ferner ist zu bemerken, daSsetzt man die beiden Bruchenden wieder zusammenein kleines Faserstuckchen fehlen muDte, namlich das in der Kerbe enthaltene Material. Dieses konnte bei dem schlagartigen Restbruchvorgang abgesprengt worden sein.

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Bioactive polymers. XIII. Carrier nature and the insolubilization conditions of enzymes

Dumitriu¹,

Bulacovschi²,

Baston³

et al. 1984

Acta Polymerica

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Les Polymères Bioactifs XI. Insolubilisation de la β‐Amylase Sur les Dérivés de la Cellulose

Bouzaher¹,

Dumitriu²,

Simionescu³

1982

Bulletin des Soc Chimique

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The immobilization of 6-amylase on acid chloride of carboxvmethylcellulose (DS = 2.02) and BIOZAN R is presented. Kinetic studies established the following conditions for a optimum coupling : pH = 8.4, time = 2 h, temperature = 5°C. The immobilization on BIOZAN R was carried out by usinq the BIOZAN R acid chloride or by activation with dicyclocarbodiimide. The results showed that the nature of the carrier and the method of immobilization determine directly the quantity and the activity of the coupled 6-amylase. INTRODUCTIONLes enzymes insolubilisees representent de nos jours un domaine de recherche trss vaste qui ne fait que se developper au fil des annees. Vue la diversification des mBthodes d'immobilisation d'enzymes et les supports qui les lient, elles trouvent des champs d'application trss importants en analvse" 2, en biochimie c o m e modsles des reactions cellulaires3' 4, en et surtout en chimie alimentaire'. Les supports utilises sont soit svnthetiques, soit naturels. Un interst particulier est accord6 aux derives de la cellulose. Parmi ceux constamment employes il y a la 4-aminobenzovlcellulose, la 4-aminobenzyl-

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Bioactive polymers XXIX—immobilisation of α‐amylase on Biozan R

Dumitriu¹,

Popa²

1985

Brit. Poly. J.

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The immobilisation of α‐amylase (E.C.3.2.1.1) on Biozan R with dicyclohexyl carbodiimide as an activator has been studied. The reaction was proved to be influenced by the enzyme support and activator support ratios as well as by the reaction duration. The function correlating the coupled enzyme activity with process parameters was derived by processing the experimental results obtained by means of a second order, composite, centrate, rotatable experimental design, using the multiple regression method. The activity of the coupled enzyme was dependent on the temperature and pH of the incubation reaction. The Michaelis‐Menten constant is higher for the immobilised enzyme as compared with the free one.

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Polymères Bioactifs X. Insolubilisation de la β‐Amylase sur des Dérivés de la Cellulose

Cited by 5 publications

References 4 publications

Bioactive polymers. XIII. Carrier nature and the insolubilization conditions of enzymes

Bioactive polymers. XIII. Carrier nature and the insolubilization conditions of enzymes

Les Polymères Bioactifs XI. Insolubilisation de la β‐Amylase Sur les Dérivés de la Cellulose

Bioactive polymers XXIX—immobilisation of α‐amylase on Biozan R

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