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
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About This Item
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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
Regulatory Information
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H Han et al.
Wei sheng wu xue bao = Acta microbiologica Sinica, 41(2), 204-208 (2003-01-29)
The extracellular penicillin acylase from Bacillus megaterium was immobilized on oxirane group of Eupergit C beads. The apparent activity of the immobilized enzyme was about 1400 u.g-1 (dry weight). The optimal pH and temperature were 8.0 and 55 degrees C
Zorica D Knezević-Jugović et al.
Methods in molecular biology (Clifton, N.J.), 679, 99-111 (2010-09-25)
A selection of the best combination of adequate immobilization support and efficient immobilization method is still a key requirement for successful application of immobilized enzymes on the industrial level. Eupergit) supports exhibit good mechanical and chemical properties and allow establishment
F Zambianchi et al.
Biotechnology and bioengineering, 78(5), 489-496 (2002-07-13)
The performance, in Baeyer-Villiger and heteroatom oxidations, of a partially purified preparation of cyclohexanone monooxygenase obtained from an Escherichia coli strain in which the gene of the enzyme was cloned and overexpressed was investigated. As model reactions, the oxidations of
Maobing Tu et al.
Biotechnology letters, 28(3), 151-156 (2006-02-21)
beta-Glucosidase is frequently used to supplement cellulase preparations for hydrolysis of cellulosic and lignocellulosic substrates in order to accelerate the conversion of cellobiose to glucose. Typically, commercial cellulase preparations are deficient in this enzyme and accumulation of cellobiose leads to
Luuk M Van Langen et al.
Biotechnology and bioengineering, 79(2), 224-228 (2002-07-13)
Native and immobilized preparations of penicillin acylase from Escherichia coli and Alcaligenes faecalis were studied using an active site titration technique. Knowledge of the number of active sites allowed the calculation of the average turnover rate of the enzyme in
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