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Merck
CN

01824

Acylase I, immobilized on Eupergit® C from Aspergillus sp.

≥50 U/g moist material

Synonym(s):

Aminoacylase, immobilized, Plexazym® AC

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About This Item

UNSPSC Code:
12352204
MDL number:
EC Number:
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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

Storage Class

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

常规特殊物品
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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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