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O7628

Sigma-Aldrich

Eupergit® C

~150 μm (macroporous particles)

Synonym(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

CAS Number:
MDL number:
UNSPSC Code:
13111000

extent of labeling

~800 μmol per g

matrix spacer

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

particle size

~150 μm (macroporous particles)

storage temp.

−20°C

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Other Notes

Matrix: hydrophilic acrylic beads

Legal Information

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

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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
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
Linus Olofsson et al.
Biotechnology letters, 28(12), 929-935 (2006-06-16)
The effects of the water-miscible organic solvents (methanol, ethanol, 1-propanol, 2-propanol, acetonitrile, N,N'-dimethylformamide and tetrahydrofuran) on the stability and catalytic activity of alpha-chymotrypsin (CT) immobilized on Eupergit CM were studied. Enhanced stabilities and activities were observed both as a consequence
L Lloret et al.
Journal of biotechnology, 162(4), 404-406 (2012-05-02)
The feasibility of the operation of a fluidized bed reactor for the removal of estrogens by immobilized laccase was investigated in order to improve the degradation yields and enzyme stability previously obtained with packed bed reactors. High removal levels (between
L Lloret et al.
Biodegradation, 23(3), 373-386 (2011-11-01)
Laccase from Myceliophthora thermophila was covalently immobilised on Eupergit C and Eupergit C 250L yielding specific activities of up to 17 and 80 U/g, respectively. Due to its superior activity, Eupergit C 250L was chosen for further research. The somewhat

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