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
13 - Non Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Solid Phase Biochemistry, 393-393 (1983)
Preparation and properties of enzymes immobilized by copolymerization.
Methods in enzymology, 44, 195-120 (1976-01-01)
Chemie Ingenieur Technik, 52, 607-607 (1980)
Optical resolution of racemic amino acids by aminoacylase.
Bioprocess technology, 16, 3-14 (1993-01-01)
Bioresource technology, 101(16), 6569-6571 (2010-04-07)
The effects of bovine serum albumin (BSA) addition on the cross-linked enzyme aggregates (CLEA) of aminoacylase from Aspergillus melleus (EC 3.5.1.14) were conducted at varying glutaraldehyde to enzyme ratio. After optimization, CLEA of aminoacylase prepared with 10 mg BSA per
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