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Documenti fondamentali

O7628

Sigma-Aldrich

Eupergit® C

~150 μm (macroporous particles)

Sinonimo/i:

Copolymer of methacrylamide, N,N′-methylen-bis(acrylamide) and a monomer carrying oxirane groups, Epoxide polymer-bound, Oxirane acrylic beads

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About This Item

Numero CAS:
Numero MDL:
Codice UNSPSC:
13111000

Prezzi e disponibilità al momento non sono disponibili

Grado di funzionalizzazione

~800 μmol per g

Braccio spaziatore

3 atoms (when ligands are coupled through the free oxirane groups. Linkage is electroneutral.)

Dimensione particelle

~150 μm (macroporous particles)

Temperatura di conservazione

−20°C

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Altre note

Matrix: hydrophilic acrylic beads

Note legali

Eupergit is a registered trademark of Röhm GmbH & Co. KG

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


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Michiel H A Janssen et al.
Biotechnology and bioengineering, 78(4), 425-432 (2002-04-12)
Penicillin G acylase from Escherichia coli was immobilized on Eupergit C with different enzyme loading. The activity of the immobilized preparations was assayed in the hydrolysis of penicillin G and was found to be much lower than would be expected
Salwa Karboune et al.
Journal of biotechnology, 120(3), 273-283 (2005-08-10)
Chlorophyllase extract from Phaeodactylum tricornutum was immobilized by physical adsorption on DEAE-cellulose and silica gel as well as by covalent binding on Eupergit C, Eupergit C250L, Eupergit C/ethylenediamine (EDA) and Eupergit C250L/EDA. Although the highest immobilization yield (83-93%) and efficiency
S S Tan et al.
Bioresource technology, 99(1), 200-204 (2007-01-30)
In this study, a thermostable recombinant xylanase B (XynB) from Thermotoga maritima MSB8 was immobilized on nickel-chelated Eupergit C 250L. This immobilized XynB was then used to hydrolyze the autohydrolysis explosion liquor of corncob (AELC) in a packed-bed enzyme reactor
Caterina Temporini et al.
Biomacromolecules, 11(6), 1623-1632 (2010-05-14)
An innovative approach to determine the orientation of penicillin G acylase (PGA) from Escherichia coli covalently immobilized onto solid supports has been developed. This method is based on tryptic digestion of immobilized PGA followed by HPLC-MS analysis of the released
Rihui Lin et al.
Preparative biochemistry & biotechnology, 41(2), 154-165 (2011-03-29)
Oxalate decarboxylase, an oxalate degradation enzyme used for medical diagnosis and decreasing the oxalate level in the food or paper industry, was covalently immobilized to Eupergit C. Different immobilization parameters, including ratio of enzyme to support, ammonia sulfate concentration, pH

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