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
Recommended Products
form
beads
specific activity
≥50 U/g moist material
storage temp.
2-8°C
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General description
the immobilized acylase catalyzes the hydrolysis of N-acetyl-DL-amino acid to L-amino acid, the D-form is not attacked
Unit Definition
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
Reconstitution
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
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 Code
13 - Non 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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Preparation and properties of enzymes immobilized by copolymerization.
D Jaworek et al.
Methods in enzymology, 44, 195-120 (1976-01-01)
J. Tramper
Solid Phase Biochemistry, 393-393 (1983)
W. Kuhlmann et al.
Chemie Ingenieur Technik, 52, 607-607 (1980)
Rainer Wardenga et al.
Applied microbiology and biotechnology, 81(4), 721-729 (2008-09-26)
Efficient recombinant expression of N-acyl-L-aminoacylase 1 from pig kidney (pAcy1) was achieved in the prokaryotic host Escherichia coli. An optimized nucleotide sequence (codon adaptation index 0.95 for E. coli), was cloned into vector pET-52(b) yielding an E. coli-expressible pAcy1 gene.
Motomu Nishioka et al.
Biotechnology letters, 30(9), 1639-1643 (2008-04-23)
Recombinant L-aminoacylase (PhoACY) from a hyperthermophilic archeon, Pyrococcus horikoshii, is a zinc-containing metalloenzyme. When the zinc was substituted by Mn(2+) or Ni(2+), its specific activity was significantly increased with acetyl-L-methionine as a substrate. The thermostability of PhoACY was improved when
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