01818
Acylase I from Aspergillus melleus
powder, brown, >0.5 U/mg
Synonym(s):
Acylase ‘Amano’, Aminoacylase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-732-3
MDL number:
Product Name
Acylase I from Aspergillus melleus, powder, brown, >0.5 U/mg
form
powder
specific activity
>0.5 U/mg
color
brown
storage temp.
2-8°C
Quality Level
Analysis Note
Enzyme activity: the optimum temperature is 40-45°C, the optimum pH is 8.0 (stable form pH 6-10). The enzyme is activated by CoCl2 in the range of 10-4 to 10-3 M.
Application
Acylase I from Aspergillus melleus has been used to catalyze the Mannich reaction.
Biochem/physiol Actions
Acylase I plays an important role in the amino acid metabolism of organisms. It also plays a role in the acylation of primary and secondary alcohols. Acylase I is involved in alcoholysis.
General description
Acylase I belongs to the aminoacylase family of enzymes.
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 37°C
Resolution of acetyl amino acids
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Preparation of the enantiomers of 1-phenylethan-1, 2-diol. Regio-and enantioselectivity of acylase I and Candida antarctica lipases A and B
Virsu P, et al.
Tetrahedron, 12(17), 2447-2455 (2001)
Enzyme-catalyzed asymmetric Mannich reaction using acylase from Aspergillus melleus
Guan Z, et al.
Journal of Molecular Catalysis. B, Enzymatic, 111, 16-20 (2015)
K. Uchida et al.
Journal of Labelled Compounds & Radiopharmaceuticals, 29, 867-867 (1991)
Physicochemical and catalytic properties of acylase I from aspergillus melleus immobilized on amino- and carbonyl-grafted stober silica
Kolodziejczak-Radzimska A, et al.
Biotechnology Progress, 767-777 (2018)
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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