form
beads
specific activity
≥50 U/g moist material
storage temp.
2-8°C
General description
the immobilized acylase catalyzes the hydrolysis of N-acetyl-DL-amino acid to L-amino acid, the D-form is not attacked
Preparation Note
Standard procedure: a 10-20% substrate solution, pH 6-8, with an addition of CoCl2 (10-4 moles) at 33°C was used. Prior to use the polymer was washed with water (50 times bed volumes); when used in a fixed bed reactor, a velocity of flow of 3 bed volumes/h leads to a hydrolysis degree of 80%
Analysis Note
moist pearls (dried substance ~30%, pearl diameter 50-100 μm), covalent fixation of the acylase
Other Notes
1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol N-acetyl-L-methionine per minute at pH 8.0 and 25°C
The immobilized acylase is used for the convenient resolution of amino acids via the selective deacetylation of N-acetyl-L-amino acids in DL-racemates
Legal Information
Eupergit is a registered trademark of Röhm GmbH & Co. KG
Plexazym is a registered trademark of Röhm GmbH & Co. KG
存储类别
13 - Non 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
常规特殊物品
此项目有
J. Tramper
Solid Phase Biochemistry, 393-393 (1983)
W. Kuhlmann et al.
Chemie Ingenieur Technik, 52, 607-607 (1980)
Preparation and properties of enzymes immobilized by copolymerization.
D Jaworek et al.
Methods in enzymology, 44, 195-120 (1976-01-01)
Optical resolution of racemic amino acids by aminoacylase.
T Sato et al.
Bioprocess technology, 16, 3-14 (1993-01-01)
Christoph M Ernst et al.
Molecular microbiology, 80(2), 290-299 (2011-02-11)
Bacteria are frequently exposed to cationic antimicrobial peptides (CAMPs) from eukaryotic hosts (host defence peptides) or from prokaryotic competitors (bacteriocins). However, many bacteria, among them most of the major human pathogens, achieve CAMP resistance by MprF, a unique enzyme that
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