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01818

Sigma-Aldrich

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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

powder

specific activity

>0.5 U/mg

color

brown

storage temp.

2-8°C

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

Pictograms

Health hazardExclamation mark

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)

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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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)
K. Uchida et al.
Journal of Labelled Compounds & Radiopharmaceuticals, 29, 867-867 (1991)
Enzyme-catalyzed asymmetric Mannich reaction using acylase from Aspergillus melleus
Guan Z, et al.
Journal of Molecular Catalysis. B, Enzymatic, 111, 16-20 (2015)
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)
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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