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Merck

61305

Sigma-Aldrich

Penicillinase from Bacillus cereus

lyophilized, powder, white, ~13 U/mg

Sinónimos:

β-Lactamase I from Bacillus cereus, β-Lactamase II, Cephalosporinase, Penicillin amido-β-lactam hydrolase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Bacillus sp. (Bacillus cereus)

Quality Level

form

powder

quality

lyophilized

specific activity

~13 U/mg

mol wt

Mr ~30000

technique(s)

activity assay: suitable

color

white

suitability

suitable for component for culture media

application(s)

diagnostic assay manufacturing

foreign activity

β-lactamase II ≤2%

storage temp.

−20°C

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General description

Penicillinase from Bacillus cereus is both an extracellular and cell-bound enzyme. It has a single polypeptide chain and has a molecular weight of 31 kDa. It lacks cysteine in the protein sequence.

Application

Penicillinase from Bacillus cereus may be used in the preparation of biosensor for amperometric detection of hydrolysis of penicillin.
Used in the production of penicillin.

Biochem/physiol Actions

Penicillinase specifically catalyzes the hydrolysis of β-lactam ring of penicillin.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Unit Definition

One unit will hydrolyze 1.0 μmole of indicated substrate per min at pH 7.0 at 25 °C. Sold as benzylpenicillin units. This International Unit (using benzylpenicillin as substrate) is approximately equal to 600 Levy or 75 Pollock units.

Other Notes

Used to destroy β-lactam antibiotics in body fluids or culture media. For the determination of penicillin; In the coupled enzyme assay for isopenicillin N synthetase; ELISA of estradiol; Penicillinase optodes

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1 - Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


Certificados de análisis (COA)

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Visite la Librería de documentos

J E Baldwin et al.
Analytical biochemistry, 145(1), 183-187 (1985-02-15)
The development of a coupled enzyme assay for the determination of isopenicillin N synthetase activity in purified extracts from Cephalosporium acremonium was described. Isopenicillin N formed from its precursor, delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV), by the synthetase was hydrolyzed by beta-lactamase I to
W. Hobel et al.
Biosensors And Bioelectronics, 7, 549-549 (1992)
Penicillinase-based amperometric biosensor for penicillin G
Gonccalves LM, et al.
Electrochemical Communications, 38, 131-133 (2014)
Properties of penicillinase from Bacillus cereus 569
Imsande J, et al.
The Journal of Biological Chemistry, 245(9), 2205-2212 (1970)
T. Scheper et al.
Analytica Chimica Acta, 163, 111-111 (1984)

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