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Documentos Principais

O7628

Sigma-Aldrich

Eupergit® C

~150 μm (macroporous particles)

Sinônimo(s):

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

Número CAS:
Número MDL:
Código UNSPSC:
13111000

Extensão da rotulagem

~800 μmol per g

espaçador de matriz

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

tamanho de partícula

~150 μm (macroporous particles)

temperatura de armazenamento

−20°C

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Outras notas

Matrix: hydrophilic acrylic beads

Informações legais

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

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, type N95 (US)


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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
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
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
Aránzazu Gómez de Segura et al.
Biotechnology progress, 20(5), 1414-1420 (2004-10-02)
Dextransucrase from Leuconostoc mesenteroides B-512F was immobilized on epoxy-activated acrylic polymers with different textural properties (Eupergit C and Eupergit C 250L). Prior to immobilization, dextransucrase was treated with dextranase to remove the dextran layer covering the enzyme surface, thus increasing
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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