O7628
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
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
Other Notes
Matrix: hydrophilic acrylic beads
Legal Information
Eupergit is a registered trademark of Röhm GmbH & Co. KG
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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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
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
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
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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