O7628
Eupergit® C
~150 μm (macroporous particles)
别名:
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
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
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
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
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