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Key Documents

01824

Sigma-Aldrich

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

Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204

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

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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J. Tramper
Solid Phase Biochemistry, 393-393 (1983)
Preparation and properties of enzymes immobilized by copolymerization.
D Jaworek et al.
Methods in enzymology, 44, 195-120 (1976-01-01)
W. Kuhlmann et al.
Chemie Ingenieur Technik, 52, 607-607 (1980)
Optical resolution of racemic amino acids by aminoacylase.
T Sato et al.
Bioprocess technology, 16, 3-14 (1993-01-01)
Tao Dong et al.
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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