01818
Acylase I from Aspergillus melleus
powder, brown, >0.5 U/mg
Synonym(s):
Acylase ‘Amano’, Aminoacylase
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About This Item
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General description
Acylase I belongs to the aminoacylase family of enzymes.
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.
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 37°C
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.
Other Notes
Resolution of acetyl amino acids
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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.
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Enzyme-catalyzed asymmetric Mannich reaction using acylase from Aspergillus melleus
Guan Z, et al.
Journal of Molecular Catalysis. B, Enzymatic, 111, 16-20 (2015)
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)
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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